2016年12月, 波紋President Choice, 中性子／X線結晶構造解析によって明らかとなった反転型セルロース加水分解酵素のプロトン伝達経路を含んだ反応機構, 日本中性子科学会
中村彰彦、石田卓也、日下勝弘、田中伊知朗、新村信雄、鮫島正浩、五十嵐圭日子
学会誌・学術雑誌による顕彰

SIRT5 mutants reveal the role of conserved asparagine and glutamine residues in the NAD+-binding pocket.
Takeshi Yokoyama; Yuki Takayama; Mineyuki Mizuguchi; Yuko Nabeshima; Katsuhiro Kusaka, SIRT5, one of the mammalian sirtuins, specifically recognizes succinyl-lysine residues on proteins and catalyzes the desuccinylation reaction. In this study, we characterized SIRT5 mutants with hydrophobic amino acid substitutions at Q140 and N141, in addition to the catalytic residue H158, known as an active site residue, by the Michaelis-Menten analysis and X-ray crystallography. Kinetic analysis showed that the catalytic efficiency (kcat/Km) of the Q140L and N141V mutants decreased to 0.02 times and 0.0038 times that of the wild-type SIRT5, respectively, with the activity of the N141V mutant becoming comparable to that of the H158M mutant. Our findings indicate that N141 contributes significantly to the desuccinylation reaction.
FEBS letters, 2024年06月20日

Resveratrol Derivatives Inhibit Transthyretin Fibrillization: Structural Insights into the Interactions between Resveratrol Derivatives and Transthyretin.
Takeshi Yokoyama; Katsuhiro Kusaka; Mineyuki Mizuguchi; Yuko Nabeshima; Satoru Fujiwara, Hereditary ATTR amyloidosis is a disease caused by the deposition of amyloid fibrils formed by mutated transthyretin (TTR), a protein that binds to thyroid hormone in the serum, in the organs. The development of a small molecule that binds to and stabilizes TTR is a promising strategy for the treatment of ATTR amyloidosis. In the present study, we demonstrated that the resveratrol derivatives including pterostilbene available as a dietary supplement inhibit the fibrillization of V30M-TTR to the same extent as the approved drug tafamidis. Furthermore, based on a thermodynamic and X-ray crystallographic analysis, the binding of the resveratrol derivative to TTR was shown to be enthalpy-driven, with the binding enthalpy being acquired by hydrogen bonding to S117. Moreover, direct observation of hydrogen atoms by neutron crystallography provided details of the hydrogen bond network by S117 and emphasized the importance of the CH···π interaction by L110 in the ligand binding.
Journal of medicinal chemistry, 2023年11月01日

〔主要な業績〕Site-specific relaxation of peptide bond planarity induced by electrically attracted proton/deuteron observed by neutron crystallography
Kaori Chiba; Takuro Matsui; Toshiyuki Chatake; Takashi Ohhara; Ichiro Tanaka; Katsuhide Yutani; Nobuo Niimura, Abstract

In structural biology, peptide bonds, fundamental linkages between hundreds of amino acids, of which a protein molecule is composed, have been commonly treated as a plane structure just as Linus Pauling et al. proposed. In this paper, a site‐specific peptide bond relaxation mechanism by deuterons whose localization has been suggested by neutron crystallography is proposed. Such deuteron was observed as an arm of neutron scattering length density protruding from the carbonyl oxygen atoms in the main chain in the omit map drawn by neutron crystallography of human lysozyme. Our comprehensive study using X‐ray and neutron diffraction and ¹⁵N chemical shifts of individual amide nitrogen atoms within the same peptide bond strongly suggests the relaxation of the electronic resonance structure because of site‐specific modulation by protons/deuterons localized on the electron orbital of the carbonyl oxygen. All experimental data used in this examination were obtained at room temperature, which is preferable for enzymatic activity. Such a close interaction between the electron resonance structure of a peptide bond and the exchangeable protons/deuterons well agreed with that observed in an intermediate state in an amide hydrolytic reaction simulated by the ab‐initio calculation including water molecules.

This article is protected by copyright. All rights reserved., Wiley
Protein Science, 2023年09月20日, ［査読有り］

Neutron Crystallography of a Semiquinone Radical Intermediate of Copper Amine Oxidase Reveals a Substrate-Assisted Conformational Change of the Peptidyl Quinone Cofactor
Takeshi Murakawa; Kazuo Kurihara; Mitsuo Shoji; Naomine Yano; Katsuhiro Kusaka; Yoshiaki Kawano; Mamoru Suzuki; Yasuteru Shigeta; Takato Yano; Motoyasu Adachi; Katsuyuki Tanizawa; Toshihide Okajima, American Chemical Society (ACS)
ACS Catalysis, 2023年09月07日

〔主要な業績〕結晶核数の制御が可能なタンパク質大形単結晶育成のための微小流路デバイスシステム
田中伊知朗, 筆頭著者, 公益社団法人日本薬学会
ファルマシア, 2023年09月01日, ［招待有り］

Rafoxanide, a salicylanilide anthelmintic, interacts with human plasma protein transthyretin.
Takeshi Yokoyama; Mineyuki Mizuguchi; Yuko Nabeshima; Yusuke Nakagawa; Takuya Okada; Naoki Toyooka; Katsuhiro Kusaka, Transthyretin (TTR) is a carrier protein for thyroid hormone thyroxine (T4 ) in plasma, placental cytosol, and cerebrospinal fluid. While the potential toxicity of small molecules that compete with T4 for binding to TTR should be carefully studied, these small molecules can also serve as anti-ATTR amyloidosis drugs by stabilizing the TTR structure. Here, we demonstrated that rafoxanide, an EU-approved anthelmintic drug for domesticated animals, binds to the T4 -binding site of TTR. An intrinsic fluorescence quenching assay showed that rafoxanide also binds to the thyroid hormone-related proteins, including serum albumin and thyroid hormone receptor β. Rafoxanide strongly inhibited TTR amyloidogenesis in fibrillization assay, but the binding of rafoxanide to TTR was interfered with in human plasma, probably due to interactions with thyroid hormone-related proteins. Protein crystallography provided clues for the optimization of binding affinity and selectivity. Our findings emphasize the importance of considering rafoxanide as both a possible thyroid-disrupting chemical and a lead compound for the development of new ATTR amyloidosis inhibitors.
The FEBS journal, 2023年07月31日

New insights into the oxidation process from neutron and X-ray crystal structures of an O₂-sensitive [NiFe]-hydrogenase
Takeshi Hiromoto; Koji Nishikawa; Seiya Inoue; Hideaki Ogata; Yuta Hori; Katsuhiro Kusaka; Yu Hirano; Kazuo Kurihara; Yasuteru Shigeta; Taro Tamada; Yoshiki Higuchi, We report the first neutron structure of [NiFe]-hydrogenase in its oxidized state. This study leads to new insights into the oxidized active site and visualization of the protons characteristic of the oxidized enzyme., Royal Society of Chemistry (RSC)
Chemical Science, 2023年

Charge neutralization and β-elimination cleavage mechanism of family 42 L-rhamnose-α-1,4-D-glucuronate lyase revealed using neutron crystallography
Naomine Yano; Tatsuya Kondo; Katsuhiro Kusaka; Taro Yamada; Takatoshi Arakawa; Tatsuji Sakamoto; Shinya Fushinobu, Abstract

Gum arabic (GA) is widely used as an emulsion stabilizer and edible coating, and consists of a complex carbohydrate moiety with a rhamnosyl-glucuronate group capping the non-reducing ends. Enzymes that can specifically cleave the glycosidic chains of GA and modify their properties are valuable tools for structural analysis and industrial application. Cryogenic X-ray crystal structure of GA-specific L-rhamnose-α-1,4-D-glucuronate lyase from Fusarium oxysporum (FoRham1), belonging to the polysaccharide lyase (PL) family 42, has been previously reported. To determine the specific reaction mechanism based on its hydrogen-containing enzyme structure, we performed joint X-ray/neutron crystallography of FoRham1. Large crystals were grown in the presence of L-rhamnose (a reaction product), and neutron and X-ray diffraction datasets were collected at room temperature up to 1.80 and 1.25 Å resolutions, respectively. The active site contained L-rhamnose and acetate, the latter being a partial analog of glucuronate. Incomplete H/D exchange between Arg166 and acetate suggested that a strong salt-bridge interaction was maintained. Doubly deuteronated His105 and deuteronated Tyr150 supported this interaction. The unusually hydrogen-rich environment functions as a charge neutralizer for glucuronate and stabilizes the oxyanion intermediate. The NE2 atom of His85 was deprotonated and formed a hydrogen bond with the deuterated O1 hydroxy of L-rhamnose, indicating the function of His85 as the base/acid catalyst for bond cleavage via β-elimination. Asp83 functions as a pivot between the two catalytic histidine residues by bridging them, and this His–His–Asp structural motif is conserved in the three PL families.

Significance Statement

Although hydrogen transfer plays an important role in enzymatic reactions, hydrogen atoms are generally invisible in macromolecular X-ray crystallography. In the reaction of polysaccharide lyases, substrate activation by negative charge stabilization of uronic acid and base/acid catalyzed β-elimination reaction have been postulated. Here, we report the neutron crystallography of polysaccharide lyase. Joint X-ray/neutron crystallography of L-rhamnose-α-1,4D-glucuronate lyase from Fusarium oxysporum (FoRham1) complexed with L-rhamnose was performed, and the hydrogen and deuterium atoms were visualized at a high resolution. FoRham1 catalyzes the specific cleavage of the cap structure of gum arabic, which is useful for various applications in the food, cosmetic, and pharmaceutical industries. A detailed catalytic mechanism for FoRham1 was proposed based on the key structural features of its active site.
bioRxiv, 2022年08月

〔主要な業績〕タンパク質大形単結晶育成のための生成結晶核数制御を可能とする微小流路デバイスシステム　　　　　　　　　　　　　　　
田中伊知朗、長谷川智紀、齋藤洋也、新村信雄、山田貢、吉崎泉、真栄城正寿、蛭田佳樹, 筆頭著者
化学工業, 2022年08月01日, ［招待有り］

〔主要な業績〕Protonation states of hen egg-white lysozyme observed using D/H contrast neutron crystallography
Toshiyuki Chatake*; Ichiro Tanaka; Katsuhiro Kusaka; Satoru Fujiwara, IUCr
Acta Cryst. D, 2022年06月01日, ［査読有り］

Revisiting the concept of peptide bond planarity in an iron-sulfur protein by neutron structure analysis
Yuya Hanazono; Yu Hirano; Kazuki Takeda; Katsuhiro Kusaka; Taro Tamada; Kunio Miki, The planarity of the peptide bond is important for the stability and structure formation of proteins. However, substantial distortion of peptide bonds has been reported in several high-resolution structures and computational analyses. To investigate the peptide bond planarity, including hydrogen atoms, we report a 1.2-Å resolution neutron structure of the oxidized form of high-potential iron-sulfur protein. This high-resolution neutron structure shows that the nucleus positions of the amide protons deviate from the peptide plane and shift toward the acceptors. The planarity of the H─N─C═O plane depends strongly on the pyramidalization of the nitrogen atom. Moreover, the orientation of the amide proton of Cys ⁷⁵ is different in the reduced and oxidized states, possibly because of the electron storage capacity of the iron-sulfur cluster., American Association for the Advancement of Science (AAAS)
Science Advances, 2022年05月20日, ［査読有り］

Re-evaluation of protein neutron crystallography with and without X-ray/neutron joint refinement
Takeshi Murakawa; Kazuo Kurihara; Motoyasu Adachi; Katsuhiro Kusaka; Katsuyuki Tanizawa; Toshihide Okajima, Protein neutron crystallography is a powerful technique to determine the positions of H atoms, providing crucial biochemical information such as the protonation states of catalytic groups and the geometry of hydrogen bonds. Recently, the crystal structure of a bacterial copper amine oxidase was determined by joint refinement using X-ray and neutron diffraction data sets at resolutions of 1.14 and 1.72 Å, respectively [Murakawa et al. (2020). Proc. Natl Acad. Sci. USA, 117, 10818–10824]. While joint refinement is effective for the determination of the accurate positions of heavy atoms on the basis of the electron density, the structural information on light atoms (hydrogen and deuterium) derived from the neutron diffraction data might be affected by the X-ray data. To unravel the information included in the neutron diffraction data, the structure determination was conducted again using only the neutron diffraction data at 1.72 Å resolution and the results were compared with those obtained in the previous study. Most H and D atoms were identified at essentially the same positions in both the neutron-only and the X-ray/neutron joint refinements. Nevertheless, neutron-only refinement was found to be less effective than joint refinement in providing very accurate heavy-atom coordinates that lead to significant improvement of the neutron scattering length density map, especially for the active-site cofactor. Consequently, it was confirmed that X-ray/neutron joint refinement is crucial for determination of the real chemical structure of the catalytic site of the enzyme., International Union of Crystallography (IUCr)
IUCrJ, 2022年05月01日, ［査読有り］

〔主要な業績〕Recent Structural Insights on the Mechanism of Lysozyme Hydrolysis
Ichiro Tanaka*; Ryota Nishinomiya; Ryosuke Goto; Shun Shimazaki; Toshiyuki Chatake, 筆頭著者, Lysozyme hydrolyzes the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycans located in the bacterial cell wall. The mechanism of the hydrolysis reaction of lysozyme was first studied more than 50 years ago; however, it has not yet been fully elucidated and various mechanisms are still being investigated. One reaction system that has commonly been proposed is that the lysozyme intermediate undergoes covalent ligand binding during hydrolysis. However, these findings resulted from experiments performed under laboratory conditions using fluorine-based ligands, which facilitate the formation of covalent bonds between the ligands and the catalytic side chain of lysozyme. More recently, high-resolution X-ray structural analysis was used to study the complex of lysozyme with an N-acetylglucosamine tetramer. As a result, the carboxyl group of Asp52 was found to form a relatively strong hydrogen-bond network and had difficulty binding covalently to C1 of the carbohydrate ring. To confirm this hydrogen-bond network, neutron test measurements were successfully performed to a resolution of better than 1.9 Å., IUCr
Acta Cryst. D, 2021年02月, ［査読有り］

〔主要な業績〕Dissolution, Mechanical Properties, and Thermal Stability of Microparticles Containing Radioactive Cesium on Plant Litter Derived from the Fukushima Daiichi Nuclear Power Plant Accident
tsushi Yamaguchi; Kenji Kikuchi; Masakazu Komatsuzaki; Ichiro Tanaka* and Nobuo Niimura, 責任著者, Most of the radioactive cesium (134Cs and 137Cs), which originated from the Fukushima Daiichi Nuclear
Power Plant (FDNPP) accident, has remained in the soil and on plants as water-insoluble microparticles
(termed as CsMPs) and maintained relatively high radioactivity levels in the district. However, it has been
reported that the radioactive Cs has been absorbed by plants. To interpret this phenomenon, the authors
investigated CsMPs to determine if they become soluble during filtration and dialysis experiments.
Moreover, other physical properties, such as mechanical properties and thermal stability, were observed
during the course of the relevant experiments. These properties can be obtained by using carbonized
charcoal litter with CsMPs., Science repository
Radiology and Medical Diagnostic Imaging, 2020年12月11日, ［査読有り］

Neutron diffraction experiment with the Y116S variant of transthyretin using iBIX at J-PARC: application of a new integration method
Katsuhiro Kusaka; Takeshi Yokoyama; Taro Yamada; Naomine Yano; Ichiro; Tanaka; Mineyuki Mizuguchi, Transthyretin (TTR) is one of more than 30 amyloidogenic proteins, and the amyloid fibrils found in patients afflicted with ATTR amyloidosis are composed of this protein. Wild-type TTR amyloids accumulate in the heart in senile systemic amyloidosis (SSA). ATTR amyloidosis occurs at a much younger age than SSA, and the affected individuals carry a TTR mutant. The naturally occurring amyloidogenic Y116S TTR variant forms more amyloid fibrils than wild-type TTR. Thus, the Y116S mutation reduces the stability of the TTR structure. A neutron diffraction experiment on Y116S TTR was performed to elucidate the mechanism of the changes in structural stability between Y116S variant and wild-type TTR through structural comparison. Large crystals of the Y116S variant were grown under optimal crystallization conditions, and a single 2.4 mm3 crystal was ultimately obtained. This crystal was subjected to time-of-flight (TOF) neutron diffraction using the IBARAKI biological crystal diffractometer (iBIX) at the Japan Proton Accelerator Research Complex, Tokai, Japan (J-PARC). A full data set for neutron structure analysis was obtained in 14 days at an operational accelerator power of 500 kW. A new integration method was developed and showed improved data statistics; the new method was applied to the reduction of the TOF diffraction data from the Y116S variant. Data reduction was completed and the integrated intensities of the Bragg reflections were obtained at 1.9 Å resolution for structure refinement. Moreover, X-ray diffraction data at 1.4 Å resolution were obtained for joint neutron-X-ray refinement.
Acta Cryst. D, 2020年11月, ［査読有り］

Towards cryogenic neutron crystallography on the reduced form of [NiFe]-hydrogenase.
Takeshi Hiromoto; Koji Nishikawa; Seiya Inoue; Hiroaki Matsuura; Yu Hirano; Kazuo Kurihara; Katsuhiro Kusaka; Matthew Cuneo; Leighton Coates; Taro Tamada; Yoshiki Higuchi, A membrane-bound hydrogenase from Desulfovibrio vulgaris Miyazaki F is a metalloenzyme that contains a binuclear Ni-Fe complex in its active site and mainly catalyzes the oxidation of molecular hydrogen to generate a proton gradient in the bacterium. The active-site Ni-Fe complex of the aerobically purified enzyme shows its inactive oxidized form, which can be reactivated through reduction by hydrogen. Here, in order to understand how the oxidized form is reactivated by hydrogen and further to directly evaluate the bridging of a hydride ligand in the reduced form of the Ni-Fe complex, a neutron structure determination was undertaken on single crystals grown in a hydrogen atmosphere. Cryogenic crystallography is being introduced into the neutron diffraction research field as it enables the trapping of short-lived intermediates and the collection of diffraction data to higher resolution. To optimize the cooling of large crystals under anaerobic conditions, the effects on crystal quality were evaluated by X-rays using two typical methods, the use of a cold nitrogen-gas stream and plunge-cooling into liquid nitrogen, and the former was found to be more effective in cooling the crystals uniformly than the latter. Neutron diffraction data for the reactivated enzyme were collected at the Japan Photon Accelerator Research Complex under cryogenic conditions, where the crystal diffracted to a resolution of 2.0 Å. A neutron diffraction experiment on the reduced form was carried out at Oak Ridge National Laboratory under cryogenic conditions and showed diffraction peaks to a resolution of 2.4 Å.
Acta crystallographica. Section D, Structural biology, 2020年10月01日

Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing.
Takeshi Murakawa; Kazuo Kurihara; Mitsuo Shoji; Chie Shibazaki; Tomoko Sunami; Taro Tamada; Naomine Yano; Taro Yamada; Katsuhiro Kusaka; Mamoru Suzuki; Yasuteru Shigeta; Ryota Kuroki; Hideyuki Hayashi; Takato Yano; Katsuyuki Tanizawa; Motoyasu Adachi; Toshihide Okajima, Recent advances in neutron crystallographic studies have provided structural bases for quantum behaviors of protons observed in enzymatic reactions. Thus, we resolved the neutron crystal structure of a bacterial copper (Cu) amine oxidase (CAO), which contains a prosthetic Cu ion and a protein-derived redox cofactor, topa quinone (TPQ). We solved hitherto unknown structures of the active site, including a keto/enolate equilibrium of the cofactor with a nonplanar quinone ring, unusual proton sharing between the cofactor and the catalytic base, and metal-induced deprotonation of a histidine residue that coordinates to the Cu. Our findings show a refined active-site structure that gives detailed information on the protonation state of dissociable groups, such as the quinone cofactor, which are critical for catalytic reactions.
Proceedings of the National Academy of Sciences of the United States of America, 2020年05月05日, ［査読有り］

〔主要な業績〕Current status and near future plan of neutron protein crystallography at J-PARC
Ichiro Tanaka; Toshiyuki Chatake; Satoru Fujiwara; Takaaki Hosoya; Katsuhiro Kusak; Nobuo Niimura; Taro Yamada; Naomine Yano, 筆頭著者, 特別号の依頼があったもので、田中が責任著者として共著者を組織し、日本唯一の執筆グループとして、J-PARCを中心としたタンパク質中性子結晶構造解析の現状と将来について、具体的な手法も含めて記述した。, Elsevier Inc.
Method in Enzymology, 2020年02月29日, ［査読有り］, ［招待有り］

High-resolution neutron crystallography visualizes an OH-bound resting state of a copper-containing nitrite reductase.
Yohta Fukuda; Yu Hirano; Katsuhiro Kusaka; Tsuyoshi Inoue; Taro Tamada, Copper-containing nitrite reductases (CuNIRs) transform nitrite to gaseous nitric oxide, which is a key process in the global nitrogen cycle. The catalytic mechanism has been extensively studied to ultimately achieve rational control of this important geobiochemical reaction. However, accumulated structural biology data show discrepancies with spectroscopic and computational studies; hence, the reaction mechanism is still controversial. In particular, the details of the proton transfer involved in it are largely unknown. This situation arises from the failure of determining positions of hydrogen atoms and protons, which play essential roles at the catalytic site of CuNIRs, even with atomic resolution X-ray crystallography. Here, we determined the 1.50 Å resolution neutron structure of a CuNIR from Geobacillus thermodenitrificans (trimer molecular mass of ∼106 kDa) in its resting state at low pH. Our neutron structure reveals the protonation states of catalytic residues (deprotonated aspartate and protonated histidine), thus providing insights into the catalytic mechanism. We found that a hydroxide ion can exist as a ligand to the catalytic Cu atom in the resting state even at a low pH. This OH-bound Cu site is unexpected from previously given X-ray structures but consistent with a reaction intermediate suggested by computational chemistry. Furthermore, the hydrogen-deuterium exchange ratio in our neutron structure suggests that the intramolecular electron transfer pathway has a hydrogen-bond jump, which is proposed by quantum chemistry. Our study can seamlessly link the structural biology to the computational chemistry of CuNIRs, boosting our understanding of the enzymes at the atomic and electronic levels., Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences of the United States of America, 2020年02月25日, ［査読有り］

Necessity and Effectiveness of a Biological Diffractometer for Installation in Second Target Station as a New Neutron Puled Source in Japan
I. Tanaka, 原子炉ＢＩＸ３，４と現在のiBIXの性能比較を行って、J-PARC MLF第2標的における蛋白質単結晶中性子回折計の必要性と有効性について、議論した。
JPS Conf. Proc., 2019年04月, ［査読有り］

Current Status and Future Prospects of Single crystal Neutron Diffractometer iBIX
Katsuhiro Kusaka; Taro Yamada; Naomine Yano; Takaaki Hosoya; Takashi Ohhara; Ichiro Tanaka, iBIXの2018年夏時点の現状についての報告と将来展望について
JPS Conf. Proc., 2019年04月, ［査読有り］

Preliminary results of neutron structural analysis of glucose isomerase under natural conditions during an enzyme reaction
S. Yamoto; N. Komatsuzaki; K. Kusaka; N. Yano; N. Okuda; Akio Sasaki; I. Tanaka, Glucose isomerase binds two divalent metals and catalyzes the isomerization of glucose to fructose. In this study, a single crystal of the ternary complex of glucose isomerase from Streptomyces rubiginosus with glucose and magnesium was prepared, and the crystal structure was analyzed under more natural reaction conditions than in previous crystallographic studies. The two histidine residues that interact with the substrate and metal in the active site were singly and doubly protonated, respectively. We also observed the glucose substrate in two molecular states, cyclic and linear, as a result of analysis of the structure under natural reaction conditions., Elsevier
Physica B, 2018年12月, ［査読有り］

Crystal Growth of a Bilin Reductase PcyA I86D Mutant-Substrate Complex for Neutron Crystallography
Keisuke Igarashi; Yoshinori Hagiwara; Masakazu Sugishima; Kei Wada; Keiichi Fukuyama; Atsushi Ikeda; Naomine Yano; Katsuhiro Kusaka; Andreas Ostermann; Masaki Unno, © 2018 American Chemical Society. Neutron crystallography of proteins requires much larger crystals than those for X-ray crystallography. Obtaining large crystals of an enzyme-substrate complex is especially difficult because strict control of the stoichiometry is needed for crystal growth. Herein is reported a procedure for obtaining crystals large enough for neutron structural analysis of a bilin reductase PcyA I86D mutant complexed with its substrate, biliverdin, an open tetrapyrrol pigment. The enzyme/substrate ratio was estimated by observing changes in absorption spectra and compared to the theoretical value; 1.2 times the amount of biliverdin was required in the experiment. This proper stoichiometric ratio of PcyA I86D mutant/biliverdin reproducibly gave high-quality crystals. The buffer for the reservoir solution in the sitting drop vapor diffusion method was chosen by analysis of Wilson plots of room temperature X-ray data of the crystals obtained using three different buffers. The mixing ratio of the PcyA I86D mutant/biliverdin complex and the crystallization solution was optimized at 9:1. These results demonstrate that optimization of the enzyme/substrate ratio as well as the crystallization solution can be an effective strategy for large crystal growth.
Crystal Growth and Design, 2018年09月05日, ［査読有り］

Structure Analysis and Derivation of Deformed Electron Density Distribution of Polydiacetylene Giant Single Crystal by the Combination of X‑ray and Neutron Diffraction Data
Kohji Tashiro; Katsuhiro Kusaka; Takaaki Hosoya; Takashi Ohhara; Makoto Hanesaka; Yoshinori Yoshizawa; Hiroko Yamamoto; Nobuo Niimura; Ichiro Tanaka; Kazuo Kurihara; Ryota Kuroki; Taro Tamada, The crystal structure of polydiacetylene giant single crystal has been analyzed on the basis of the two different methods of wide-angle neutron diffraction and X-ray diffraction. The X-ray result gives us the total electron density distribution [ρ(x)] of polymer chain. The neutron result tells the positions of atomic nuclei, which can allow us to speculate the electron density distributions [ρ0(x)] around the nonbonded isolated atoms. As a result, the so-called bonded (or deformed) electron density Δρ(x) [≡ ρ(x) - ρ0(x) = ρX(x) - ρN(x)], i.e., the electron density distribution due to the conjugation among the covalently bonded atoms along the polymer chain, can be estimated using the two information obtained by the X-ray and neutron data analyses (the so-called X-ray-neutron subtraction (X-N) method). The present report is the first example of the application of X-N method to the synthetic polymer species. The Δρ(x) derived for polydiacetylene was found similar to that of the low-molecular-weight model compound having the similar electronically conjugated chemical formula. The Δρ(x) was calculated by the density functional theory, which was in a good agreement with the experimental result qualitatively., American Chemical Society
Macromolecules, 2018年06月12日, ［査読有り］

Detection of Radioactive Cesium on Granular Particle using Autoradiography, Germanium detector and Energy dispersive X-ray spectrometry
Kenji Kikuchi; Nobuo NIIMURA; Takashi ONIZAWA; Masakazu Komatsuzaki; Ichiro Tanaka
Radiology and Diagnostic Imaging, 2018年05月25日, ［査読有り］

Protonation/deprotonation of proteins by neutron diffraction structure analysis
Ichiro Tanaka; Katsuhiro Kusaka; Nobuo Niimura, Neutron protein crystallography can reveal nuclear position and it is very useful to find hydrogen or protonation/deprotonation of protein. It is, however, an intensity-limited experiment and requires large and good quality single protein crystal, so the user population has been so small. Recently, new intense neutron source makes ones to find several protonation states in proteins
PcyA complex (complex of Phycocyanobilin: Ferredoxin Oxidoreductase and Biliverdin IXA), cellulase and substrate complex and farnesyl pyrophosphate synthase (FPPS)-drug complex. At the same time, new techniques for neutron measurement such as high pressure freezing and dynamic nuclear polarization of protein have been also tried to be developed. Finally, a plan of new neutron facility to gain more S/N ratio is expected so that the sample crystal volume can be much small to find protonation/deprotonation., Springer Singapore
The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery, 2018年05月07日

〔主要な業績〕Cryoprotectant-Free High-Pressure Freezing and Dynamic Nuclear Polarization for More Sensitive Detection of Hydrogen in Neutron Protein Crystallography　　　　　　　　　　　　　　　
Ichiro Tanaka; Naoya Komatsuzaki; Wen-Xue Yue; Toshiyuki Chatake; Katsuhiro Kusaka; Nobuo Niimura; Daisuke Miura; Takahiro Iwata; Yoshiyuki Miyachi; Genki Nukazuka; Hiroki Matsuda, 高圧凍結と動的核偏極の開発報告, IUCr
Acta Cryst. D, 2018年05月, ［査読有り］

Visualization of proton and electron transfer processes of a biochemical reaction by μSR
Tamiko KIYOTANI; Masayoshi KOBAYASHI; Ichiro TANAKA; and Nobuo NIIMURA
JPS Conf. Proc., 2018年03月, ［査読有り］

Status of neutron time-of-flight single-crystal diffraction data processing software STARGazer
Naomine Yano; Taro Yamada; Takaaki Hosoya; Takashi Ohhara; Ichiro Tanaka; Nobuo Niimura; Katsuhiro Kusaka
Acta Cryst. D, 2018年, ［査読有り］

タンパク質の高圧凍結法の汎用化　　　　　　　　　　　　　　　
杉山玲; 田中伊知朗
Photon Factory Activity Report 2016 #34, 2017年07月

リゾチーム－糖複合体の中性子構造解析に向けて　　　　　　　　　　　　　　　
後藤亮祐; 日下勝弘; 矢野直峰; 田中伊知朗
Photon Factory Activity Report 2016 #34, 2017年07月

Application of profile fitting method to neutron time-of-flight protein single crystal diffraction data collected at the iBIX
Naomine Yano; Taro Yamada; Takaaki Hosoya; Takashi Ohhara; Ichiro Tanaka; Katsuhiro Kusaka, We developed and employed a profile fitting method for the peak integration of neutron time-of-flight diffraction data collected by the IBARAKI Biological Crystal Diffractometer (iBIX) at the Japan Proton Accelerator Research Complex (J-PARC) for protein ribonuclease A and alpha-thrombin single crystals. In order to determine proper fitting functions, four asymmetric functions were evaluated using strong intensity peaks. A Gaussian convolved with two back-to-back exponentials was selected as the most suitable fitting function, and a profile fitting algorithm for the integration method was developed. The intensity and structure refinement data statistics of the profile fitting method were compared to those of the summation integration method. It was clearly demonstrated that the profile fitting method provides more accurate integrated intensities and model structures than the summation integration method at higher resolution shells. The integration component with the profile fitting method has already been implemented in the iBIX data processing software STARGazer and its user manual has been prepared., NATURE PUBLISHING GROUP
SCIENTIFIC REPORTS, 2016年12月, ［査読有り］

ORNL Tours 報告　　　　　　　　　　　　　　　
田中伊知朗
169th Committee on Diffraction Struct. Biol. News Letter, 2016年10月, ［査読有り］, ［招待有り］

中性子／X線結晶構造解析によって明らかとなった反転型セルロース加水分解酵素のプロトン伝達経路を含んだ反応機構
中村彰彦、石田卓也、日下勝弘、田中伊知朗、新村信雄、鮫島正浩、五十嵐圭日子
日本中性子科学会誌｢波紋｣, 2016年10月, ［査読有り］, ［招待有り］

Neutron and X-ray single-crystal diffraction from protein microcrystals via magnetically oriented microcrystal arrays in gels
Shu Tsukui; Fumiko Kimura; Katsuhiro Kusaka; Seiki Baba; Nobuhiro Mizuno; Tsunehisa Kimura, Protein microcrystals magnetically aligned in D2O hydrogels were subjected to neutron diffraction measurements, and reflections were observed for the first time to a resolution of 3.4 angstrom from lysozyme microcrystals (similar to 10 x 10 x 50 mu m). This result demonstrated the possibility that magnetically oriented microcrystals consolidated in D2O gels may provide a promising means to obtain single-crystal neutron diffraction from proteins that do not crystallize at the sizes required for neutron diffraction structure determination. In addition, lysozyme microcrystals aligned in H2O hydrogels allowed structure determination at a resolution of 1.76 angstrom at room temperature by X-ray diffraction. The use of gels has advantages since the microcrystals are measured under hydrated conditions., INT UNION CRYSTALLOGRAPHY
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2016年07月, ［査読有り］

Development of Experimental Techniques for Neutron Biology　　　　　　　　　　　　　　　
T. Chatake; S. Fujiwara; Y. Yanagisawa; I. Tanaka
KUR Pregrss Rep., 2016年07月

中性子/X線複合構造解析で酵素触媒反応におけるプロトンリレーを可視化する
中村彰彦,石田卓也,日下勝弘,山田太郎,田中伊知朗,新村信雄,鮫島正浩,五十嵐圭日子
生物物理学会誌, 2016年06月, ［査読有り］, ［招待有り］

生体内反応に関与するタンパク質結晶解析のための水素核の動的核偏極
三浦 大輔; 岩田 高広; 宮地 義之; 田中 伊知郎; 松田 洋樹; 糠塚 元気; 小松崎 直也,

生体内反応に関与するタンパク質の結晶構造を J-PARC の中性子を使用した回折実験によって解析が行われている。しかし非干渉性バックグラウンドが大きい等の課題があった。この課題を克服し、かつ水素検出度を向上するのにタンパク質結晶内の水素核のスピンの向きを中性子のスピンの方向と揃えることが有効であり、動的核偏極を用いて水素核の偏極実験を行った。本講演ではこの測定結果について発表する。

, 一般社団法人 日本物理学会
日本物理学会講演概要集, 2016年

Protonation State and Hydration of Bisphosphonate Bound to,Farnesyl Pyrophosphate Synthase
Takeshi Yokoyama; Mineyuki Mizuguchi; Andreas Ostermann; Katsuhiro Kusaka; Nobuo Niimura; Tabias E. Schrader; and Ichiro Tanaka, 骨粗しょう症原因タンパク質と既存の薬剤との複合体の、J-PARC iBIXによる中性子結晶構造解析を行うことにより、薬剤のリン酸基がすべてでプロトネーションしていたことがわかり、今後の薬剤開発に有用な情報を得られた。, AMER CHEMICAL SOC
J. Med. Chem., 2015年09月, ［査読有り］

Towards Direct Observation of Electron and Proton Transfers Due to Enzymatic Reaction in Trypsin by μSR　　　　　　　　　　　　　　　
Masayoshi KOBAYASHI; Ichiro TANAKA; Tamiko KIYOTANI; Nobuo NIIMURA, J-PARC MLFのミュオンビームを用いて観測を計画している、タンパク質酵素反応におけるプロトン移動に伴う微小磁場の大きさの計算を行い0.1mT程度であり、十分観測可能な量であることを示した。
JPS Conference Proc., 2015年09月, ［査読有り］

ATP Binding and Hydration State Analyses of DAPK: Steps toward Neutron Protein Crystallography Studies
Atsushi YAMAGUCHI; Nobuo NIIMURA; Shigeyoshi NAKAMURA; Shun-ichi KIDOKORO; Toshiyuki CHATAKE; Takeshi YOKOYAMA; Ichiro TANAKA, DAPKタンパク質のApo体のX線結晶構造解析、中性子解析に向けた2つのpH条件下での結晶化相図作成、さらにはDAPKの基質アナログであるADPやATPγSとの結合に関する相互作用を測定するITC観測を行い、結晶構造とITCではADPにおいて様式が異なる可能性が示唆された。
JPS Conference Proc., 2015年09月, ［査読有り］

“Newton’s cradle” proton relay with amide–imidic acid tautomerization in inverting cellulase visualized by neutron crystallography
Akihiko Nakamura; Takuya Ishida; Katsuhiro Kusaka; Taro Yamada; Shinya Fushinobu; Ichiro Tanaka; Satoshi Kaneko; Kazunori Ohta; Hiroaki Tanaka; Koji Inaka; Yoshiki Higuchi; Nobuo Niimura; Masahiro Samejima; Kiyohiko Igarashi, きのこのセルロース分解酵素であるセルラーゼの基質があるときとないときの両方の中性子結晶構造解析を行うことにより、活性部位のAsnが通常のアミド型ではなく、イミド酸型であり、プロトンを供給することにより加水分解を行うことが判明した。また、この変化が、カチカチ玉のような分子内プロトン移動によって引き起こされることも考察できた。, AMER ASSOC ADVANCEMENT SCIENCE
Sci. Adv., 2015年08月, ［査読有り］

Insights into the Proton Transfer Mechanism of a Bilin Reductase PcyA Following Neutron Crystallography
Masaki Unno; Kumiko Ishikawa-Suto; Katsuhiro Kusaka; Taro Tamada; Yoshinori Hagiwara; Masakazu Sugishima; Kei Wada; Taro Yamada; Katsuaki Tomoyori; Takaaki Hosoya; Ichiro Tanaka; Nobuo Niimura; Ryota Kuroki; Koji Inaka; Makiko Ishihara and Keiichi Fukuyama, 光合成色素合成酵素Bilin Reductase PcyAと色素原料の複合体の中性子結晶構造解析により、基質材料が２つのこうぞうを取っていることがわかり、プロトネーションの様子も判明した。また、X線損傷のないありのままの構造を捉えることができ、ヒドロニウムイオンも発見できた。, AMER CHEMICAL SOC
J. Am. Chem. Soc., 2015年04月, ［査読有り］

広角X線回折および広角中性子回折に基づく高分子結晶構造の精密解析
田代孝二; 塙坂 真; 山元博子; Kaewkan Wasanasuk; Paramita Jayaratri; 吉澤功徳; 田中伊知朗; 新村信雄; 日下勝弘; 細谷孝明; 大原高志; 栗原和男; 黒木良太; 玉田太郎; 藤原 悟; 勝部勝義; 森川佳介; 古宮行淳; 北野利明; 二宗 隆; 尾関智二, 原子炉及びパルス中性子を用いてポリマーの構造機能相関に関する水素原子位置の影響を初めて考察した。, 公益社団法人 高分子学会
高分子論文集, 2014年11月, ［査読有り］

Evaluation of intensity and pulse width of different moderators for designing a new diffractometer for protein crystals with large unit cells in J-PARC/MLF.
Katsuaki Tomoyori; Katsuhiro Kusaka; Taro Yamada; Taro Tamada, We plan to design a high-resolution biomacromolecule neutron time-of-flight diffractometer, which allows us to collect data from crystals with unit cells above 250 Å, in the materials and life science experimental facility at the Japan Proton Accelerator Research Complex. This new diffractometer can be used for a detailed analysis of large proteins such as membrane proteins and supermolecular complex. A quantitative comparison of the intensity and pulse width of a decoupled moderator (DM) against a coupled moderator (CM) considering the pulse width time resolution indicated that the DM satisfies the criteria for our diffractometer rather than the CM. The results suggested that a characteristic feature of the DM, i.e., narrow pulse width with a short tail, is crucial for the separation of Bragg reflections from crystals with large unit cells. On the other hand, it should be noted that the weak signals from the DM are buried under the high-level background caused by the incoherent scattering of hydrogen atoms, especially, in the case of large unit cells. We propose a profile-fitting integration method combined with the energy loss functions and a background subtraction method achieved by employing the statistics-sensitive nonlinear iterative peak-clipping algorithm.
Journal of structural and functional genomics, 2014年09月, ［査読有り］

Crystallization and preliminary neutron diffraction experiment of human,farnesyl pyrophosphate synthase complexed with risedronate
Takeshi Yokoyama*; Andreas Ostermann; Mineyuki Mizuguchi; Nobuo Niimura; Tobias E. Schraderand Ichiro Tanaka, 薬剤開発に向けた骨粗しょう症原因タンパク質と既存の薬剤との複合体の中性子結晶構造解析をドイツの原子炉中性子とJ-PARC iBIXによるパルス中性子によって行った。, International Union of Crystallography
Acta Cryst. F, 2014年05月, ［査読有り］

Visualization of the electron transfer associated with biochemical reaction process by the ultra-slow muon　　　　　　　　　　　　　　　
Nobuo NIIMURA; Ichiro TANAKA; Masayoshi KOBAYASHI, 酵素と基質の反応時におけるプロトンおよび電子移動がミュオン分光による磁場観測可能性を示した。
JPS Conference Proc., 2014年04月, ［査読有り］

トランスサイレチンの中性子結晶構造解析で明らかにする水素結合ネットワークとpH感受性
横山武司,水口峰之、日下勝弘,田中伊知朗,新村信雄, アミロイド病の原因となるタンパク質の中性子結晶構造解析を基に、薬品設計にまで応用ができることを示した。
日本結晶学会誌, 2014年04月, ［査読有り］

Accurate Structure Analyses of Polymer Crystals on the Basis of Wide-Angle X-ray and Neutron Diffractions
Kohji Tashiro; Makoto Hanesaka; Hiroko Yamamoto; Kaewkan Wasanasuk; Paramita Jayaratri; Yoshinori Yoshizawa; Ichiro Tanaka; Nobuo Niimura; Katsuhiro Kusaka; Takaaki Hosoya; Takashi Ohhara; Kazuo Kurihara; Ryota Kuroki; Taro Tamada; Satoru Fujiwara; Katsuyoshi Katsube; Keisuke Morikawa; Yukiatsu Komiya; Toshiaki Kitano; Takashi Nishu; Tomoji Ozeki, The crystal structure analysis of various polymer substances has been reviewed on the basis of wide-angle high-energy X-ray and neutron diffraction data. The progress in structural analytical techniques of polymer crystals have been reviewed at first. The structural models proposed so far were reinvestigated and new models have been proposed for various kinds of polymer crystals including polyethylene, poly(vinyl alcohol), poly(lactic acid) and its stereocomplex etc. The hydrogen atomic positions were also clarified by the quantitative analysis of wide-angle neutron diffraction data, from which the physical properties of polymer crystals have been evaluated theoretically. The bonded electron density distribution has been estimated for a polydiacetylene single crystal on the basis of the so-called X-N method or by the combination of structural information derived from X-ray and neutron diffraction data analysis. Some comments have been added about future developments in the field of structure-property relationship determination., SOC POLYMER SCIENCE JAPAN
KOBUNSHI RONBUNSHU, 2014年, ［査読有り］

Hydrogen-bond network and pH sensitivity in human transthyretin
Takeshi Yokoyama; Mineyuki Mizuguchi; Yuko Nabeshima; Katsuhiro Kusaka; Taro Yamada; Takaaki Hosoya; Takashi Ohhara; Kazuo Kurihara; Ichiro Tanaka; Nobuo Niimura, Transthyretin (TTR) is a tetrameric protein. TTR misfolding and aggregation are associated with human amyloid diseases. Dissociation of the TTR tetramer is believed to be the rate-limiting step in the amyloid fibril formation cascade. Low pH is known to promote dissociation into monomer and the formation of amyloid fibrils. In order to reveal the molecular mechanisms underlying pH sensitivity and structural stabilities of TTR, neutron diffraction studies were conducted using the IBARAKI Biological Crystal Diffractometer with the time-of-flight method. Crystals for the neutron diffraction experiments were grown up to 2.5 mm 3 for four months. The neutron crystal structure solved at 2.0 angstrom revealed the protonation states of His88 and the detailed hydrogen-bond network depending on the protonation states of His88. This hydrogen-bond network is involved in monomer-monomer and dimer-dimer interactions, suggesting that the double protonation of His88 by acidification breaks the hydrogen-bond network and causes the destabilization of the TTR tetramer. Structural comparison with the X-ray crystal structure at acidic pH identified the three amino acid residues responsible for the pH sensitivity of TTR. Our neutron model provides insights into the molecular stability related to amyloidosis., WILEY-BLACKWELL
JOURNAL OF SYNCHROTRON RADIATION, 2013年11月, ［査読有り］

Fundamental studies for the proton polarization technique in,neutron protein crystallography　　　　　　　　　　　　　　　
Ichiro Tanaka; Katsuhiro Kusaka; Toshiyuki Chatake; Nobuo Niimura, 生体高分子の水素位置観測のための高感度化に向けて、中性子核偏極回折実験を実現するための大型タンパク質単結晶凍結法の開発とラジカル分子導入とその定量を行い、生体高分子単結晶試料の核偏極への基礎的な段階をクリアした。企画、実験、議論を主体的に進めた。
J. Synchrotron Rad., 2013年10月, ［査読有り］

Hydrogen-bond network and pH sensitivity in human transthyretin
Takeshi Yokoyama; Mineyuki Mizuguchi; Yuko Nabeshima; Katsuhiro Kusaka; Taro Yamada; Takaaki Hosoya; Takashi Ohhara; Kazuo Kurihara; Ichiro Tanaka; Nobuo Niimura
J. Synchrotron Rad., 2013年10月, ［査読有り］, ［招待有り］

Phase-diagram-guided method for growth of a large crystal of glycoside hydrolase family 45 inverting cellulase suitable for neutron structural analysis
Akihiko Nakamura; Takuya Ishida; Shinya Fushinobu; Katsuhiro Kusaka; Ichiro Tanaka; Koji Inaka; Yoshiki Higuchi; Mika Masaki; Kazunori Ohta; Satoshi Kaneko; Nobuo Niimura; Kiyohiko Igarashi* and Masahiro Samajima, Neutron protein crystallography (NPC) is a powerful tool for determining the hydrogen position and water orientation in proteins, but a much larger protein crystal is needed for NPC than for X-ray crystallography, and thus crystal preparation is a bottleneck. To obtain large protein crystals, it is necessary to know the properties of the target protein in the crystallization solution. Here, a crystal preparation method of fungal cellulase PcCel45A is reported, guided by the phase diagram. Nucleation and precipitation conditions were determined by sitting-drop vapor diffusion. Saturation and unsaturation conditions were evaluated by monitoring crystal dissolution, and a crystallization phase diagram was obtained. To obtain a large crystal, crystallization solution was prepared on a sitting bridge (diameter = 5 mm). Initial crystallization conditions were 40 mu l of crystallization solution (40 mg ml(-1) protein with 30.5% 3-methyl-1,5-pentanediol in 50 mM tris-HCl pH 8.0) with a 1000 mu l reservoir (61% 3-methyl-1,5,pentanediol in 50 mMtris-HCl pH 8.0) at 293 K. After the first crystal appeared, the concentration of precipitant in the reservoir solution was reduced to 60% to prevent formation of further crystals. Finally, we obtained a crystal of 6 mm(3) volume (3 mm x 2 mm x 1 mm), which was suitable for neutron diffraction., WILEY-BLACKWELL
J. Synchrotron Rad., 2013年10月, ［査読有り］

Evaluation of performance for IBARAKI biological crystal diffractometer iBIX with new detectors　　　　　　　　　　　　　　　
Kusaka, K; Hosoya, T; Yamada, T; Tomoyori, K; Ohhara, T; Katagiri, M; Kurihara, K; Tanaka, I; Niimura, N
J. Synchrotron Rad., 2013年10月, ［査読有り］

Profile functions to reproduce Bragg reflection shapes observed by a time-of-flight single-crystal diffractometer installed at a coupled moderator pulsed neutron source in J-PARC
K. Tomoyori; K. Kusaka; T. Yamada; T. Hosoya; T. Ohhara; K. Kurihara; I. Tanaka; M. Katagiri; N. Niimura, パルス中性子源J-PARCに設置された生体高分子回折装置iBIXのブラッグ反射のTOF方向の反射の重なりを評価するために、結合型減速材のパルス形状から、試料単結晶のブラッグ反射プロファイルの再現を計算で実現し、観測値と良く一致させることができた。企画、実験、議論の一部を担当。
Nuclear Instruments and Methods in Physics Research A, 2013年08月, ［査読有り］

Neutron and X-ray crystallographic analysis of the human α-thrombin–bivalirudin complex at pD 5.0: Protonation states and hydration structure of the enzyme–product complex
Taro Yamada; Kazuo Kurihara; Yuki Ohnishi; Taro Tamada; Katsuaki Tomoyori; Kenji Masumi; Ichiro Tanaka; Ryota Kuroki; Nobuo Niimura, 凝血作用のあり、脳血栓防止剤のターゲットタンパク質ヒトトロンビンに、阻害剤のビバリルジンを結合させた複合体の中性子結晶構造解析を行い、基質が切れた状態のセリンプロテアーゼの加水分解機構を考察した。企画、実験、議論の一部を担当。, Elsevier B.V.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013年05月25日, ［査読有り］

Neutron and X-ray crystallographic analysis of Achromobacter protease I at pD 8.0: Protonation states and hydration structure in the free-form
Yuki Ohnishi; Taro Yamada; Kazuo Kurihara; Ichiro Tanaka; Fumio Sakiyama; Takeharu Masaki; Nobuo Niimura, リシン部位でタンパク質を特異的に加水分解するセリンプロテアーゼAPIの基質フリーでのpD8での中性子結晶構造解析より、基質切断部位のプロトネーションの特徴が判明した。企画、実験、議論の一部を担当, Elsevier B.V.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013年05月, ［査読有り］

A Functional [NiFe]Hydrogenase Mimic That Catalyzes Electron and Hydride Transfer from H-2
Seiji Ogo; Koji Ichikawa; Takahiro Kishima; Takahiro Matsumoto; Hidetaka Nakai; Katsuhiro Kusaka; Takashi Ohhara, Chemists have long sought to mimic enzymatic hydrogen activation with structurally simpler compounds. Here, we report a functional [NiFe]-based model of [NiFe] hydrogenase enzymes. This complex heterolytically activates hydrogen to form a hydride complex that is capable of reducing substrates by either hydride ion or electron transfer. Structural investigations were performed by a range of techniques, including x-ray diffraction and neutron scattering, resulting in crystal structures and the finding that the hydrido ligand is predominantly associated with the Fe center. The ligand's hydridic character is manifested in its reactivity with strong acid to liberate H-2., AMER ASSOC ADVANCEMENT SCIENCE
SCIENCE, 2013年02月, ［査読有り］

3P286 タンパク質中性子結晶構造解析におけるプロトン偏極法のための基礎的な試み(26.計測,ポスター,日本生物物理学会年会第51回(2013年度))
Ichiro Tanaka; Katsuhiro Kusaka; Toshiyuki Chatake; Nobuo Niimura, Biophysical Society of Japan
Seibutsu Butsuri, 2013年

Structure of Morpholinium Tribromoplumbate C4H8ONH2PbBr3,Studied Using Single-Crystal Neutron Diffraction　　　　　　　　　　　　　　　
Takuro KAWASAKI; Miwako TAKAHASHI; Takashi OHHARA; Ichiro TANAKA; Katsuhiro KUSAKA; Takaaki HOSOYA; Taro YAMADA; Kazuo KURIHARA, J-PARCのiBIXを用いて、鉛や臭素などの重原子を含む有機分子の水素原子の位置や温度因子を正確に決めることができた。企画、実験、執筆の一部を担当。
J. Phys. Soc. Jpn., 2012年08月, ［査読有り］

Hydrogen-bond network and pH sensitivity in transthyretin: Neutron crystalstructure of human transthyretin
Takeshi Yokoyama; Mineyuki Mizuguchi; Yuko Nabeshima; Katsuhiro Kusaka; Taro Yamada; Takaaki Hosoya; Takashi Ohhara; Kazuo Kurihara; Katsuaki Tomoyori; Ichiro Tanaka; Nobuo Niimura, Transthyretin (TTR) is a tetrameric protein associated with human amyloidosis. In vitro, the formation of amyloid fibrils by TTR is known to be promoted by low pH. Here we show the neutron structure of TTR, focusing on the hydrogen bonds, protonation states and pH sensitivities. A large crystal was prepared at pD 7.4 for neutron protein crystallography. Neutron diffraction studies were conducted using the IBA-RAKI Biological Crystal Diffractometer with the time-of-flight method. The neutron structure solved at 2.0 angstrom resolution revealed the protonation states of His88 and the detailed hydrogen-bond network depending on the protonation states of His88. This hydrogen-bond network is composed of Thr75, Trp79, His88, Ser112, Pro113, Thr118-B and four water molecules, and is involved in both monomer-monomer and dimer-dimer interactions, suggesting that the double protonation of His88 by acidification breaks the hydrogen-bond network and causes the destabilization of the TTR tetramer. In addition, the comparison with X-ray structure at pH 4.0 indicated that the protonation occurred to Asp74, His88 and Glu89 at pH 4.0. Our neutron model provides insights into the molecular stability of TTR related to the hydrogen-bond network, the pH sensitivity and the CH center dot center dot center dot O weak hydrogen bond. (C) 2012 Elsevier Inc. All rights reserved., ACADEMIC PRESS INC ELSEVIER SCIENCE
J. Struct. Biol., 2012年02月, ［査読有り］

Quaternary structure, aggregation and cytotoxicity of transthyretin
M. Mizuguchi; T. Yokoyama; Y. Nabeshima; K. Kawano; I. Tanaka; N. Niimura, アミロイド病の原因タンパク質であるトランスサイレチンの中性子解析の結果から創薬への応用の可能性を論じた。企画、実験、議論の一部を担当。, INFORMA HEALTHCARE
Amyloid, 2012年, ［査読有り］

High-resolution X-ray study of the effects of deuteration on crystal growth and the crystal structure of proteinase K
Toshiyuki Chatake; Takuya Ishikawa; Yasuhide Yanagisawa; Taro Yamada; Ichiro Tanaka; Satoru Fujiwara and Yukio Morimoro, Deuteration of macromolecules is an important technique in neutron protein crystallography. Solvent deuteration of protein crystals is carried out by replacing water (H2O) with heavy water (D2O) prior to neutron diffraction experiments in order to diminish background noise. The effects of solvent deuteration on the crystallization of proteinase K (PK) with polyethylene glycol as a precipitant were investigated using high-resolution X-ray crystallography. In previous studies, eight NO3- anions were included in the PK crystal unit cell grown in NaNO3 solution. In this study, however, the PK crystal structure did not contain NO3- anions; consequently, distortions of amino acids arising from the presence of NO3- anions were avoided in the present crystal structures. High-resolution (1.1 angstrom) X-ray diffraction studies showed that the degradation of PK crystals induced by solvent deuteration was so small that this degradation would be negligible for the purpose of neutron protein crystallography experiments at medium resolution. Comparison of the nonhydrogen structures of nondeuterated and deuterated crystal structures demonstrated very small structural differences. Moreover, a positive correlation between the root-mean-squared differences and B factors indicated that no systematic difference existed., WILEY-BLACKWELL
Acta Cryst. F, 2011年11月, ［査読有り］

Crystal Structure Analysis of Poly(L-lactic Acid) α Form On the basis of the 2-Dimensional Wide-Angle Synchrotron X-ray and Neutron Diffraction Measurements
Kaewkan Wasanasuk; TASHIRO Kohji; HANESAKA Makoto; OHHARA Takashi; KURIHARA Kazuo; KUROKI Ryota; TANAKA Ichiro; OZEKI Tomoji; KANAMOTO Tetsuo, The crystal structure of poly(L-lactic acid) (PLLA) alpha form has been analyzed in detail by utilizing the 2-dimensional wide-angle X-ray (WAXD) and neutron diffraction (WAND) data measured for the ultradrawn sample. The WAXD data were collected using a synchrotron-sourced high-energy X-ray beam of wavelength 0.328 angstrom at SPring-8, Japan and the WAND data were measured using a neutron beam of wavelength 1.510 angstrom with a cylindrical imaging-plate camera of BLX-3 system at Japan Atomic Energy Agency. The initial crystal structure model was extracted successfully by a direct method under the assumption of the space group P2(1)2(1)2(1) using about 700 X-ray reflections obgerved at -150 degrees C, the number of which was over-whelmingly large compared with the data reported by the previous other researchers and allowed us to perform more precise structural analysis. The crystal structure model obtained by the direct method was refined so that the best agreement between the observed and calculated integrated intensities was obtained or the reliability factor (R) became minimal: R was 18.2% at -150 degrees C and 23.2% at 25 degrees C. The thus-obtained chain conformation took the distorted (10/3) helical form with 2(1) helical symmetry along the chain axis. However, the symmetrically forbidden reflections 003, 007, 009 etc. were detected in a series of the 00L reflections, requiring us to erase the 2(1) screw symmetry along the molecular chain. By assuming the space group symmetry P12(1)1, the structural refinement was made furthermore and the finally obtained R factor was 19.3% at -150 degrees C and 19.4% at 25 degrees C. Although the structural deviation from the 2(1) screw symmetry was only slightly, this refined model was found to reproduce the observed reflection profiles well for all the layer lines. The thus X-ray-analyzed crystal structure was transferred to the WAND data analysis to determine the hydrogen atomic positions. The R factor was 23.0% for the 92 observed reflections at 25 degrees C. The agreement between the observed and calculated layer line profiles was good. In this way the crystal structure of PLLA alpha form has been established on the basis of both the X-ray and neutron diffraction analyses., AMER CHEMICAL SOC
Macromolecules, 2011年08月, ［査読有り］

X-ray and neutron protein crystallographic analysis of the trypsin-BPTI complex　　　　　　　　　　　　　　　
K. Kawamura; T. Yamada; K. Kurihara; T. Tamada; R. Kuroki; I. Tanaka; H. Takahashi; N. Niimura
Acta Cryst. D, 2011年03月, ［査読有り］

茨城県生命物質構造解析装置（iBIX）による水素・水和水の構造研究/産業利用
田中伊知朗; 日下勝弘; 細谷孝明; 大原高志; 栗原和男; 新村信雄,山田太郎,友寄克亮,横山武司,大西裕季,大隅孝志,内田裕久,鈴木榮一郎,柏木立己,宮本晃男,古川保典,吉村政志,河村貴宏
RADIOISOTOPES, 2011年02月, ［査読有り］

Time of Flight Neutron Diffractometer Dedicated to Structural Biology　　　　　　　　　　　　　　　
T. CHATEKE; Y. MORIMOTO; K. KUSAKA; I. TANAKA; N. NIIMURA
KENS Report, 2011年

Crystallization Phase Diagram, the Growth of Large Single Crystals of Bovine alpha-Lactoglobulin
D. Yagi; Y. Ohnishi; I. Tanaka; N. Niimura, A crystallization phase diagram defining the meta-stable region of bovine beta-lactoglobulin A (beta-Lg) was firstly determined by a dialysis method. We have succeeded in growing a large single crystal of beta-Lg by selecting a crystal grown in this "meta-stable region" method described in the present paper. The quality of protein crystals was characterized quantitatively via rapid X-ray data collections, followed by the use of Wilson plots to analyze their resulting average B-factors., IOP PUBLISHING LTD
Journal of Physics: Conference Series, 2010年12月, ［査読有り］

Current Status of IBARAKI Biological Crystal Diffractometer iBIX - Several Examples of the Measurement
Katsuhiro Kusaka; Ichiro Tanaka; Takaaki Hosoya; Kazuo Kurihara; Takashi Ohhara; Nobuo Niimura, Since 2004, Ibaraki prefecture has constructed the TOF neutron biological diffractometer (iBIX) at J-PARC for industrial use. Since the end of 2008, Ibaraki University has operated iBIX in order to support the experiment of users and to improve the instruments. The diffractometer is designed to measure samples with their cell edges up to around 150 angstrom. In the beginning of December in 2008, the basic optics, the support system of detectors and the three detectors were completed for the diffraction experiments. We have tried to measure the TOF diffraction data of several proteins and organic compounds in order to estimate the efficiency and characteristics of the diffcactometer. The TOF diffraction data of Ribonuclease A can be measured under the following conditions, beam power: 20kW, pulse repetition: 25Hz, range of wavelength: 0.5 similar to 4 angstrom, exposure time: 18.7 hours. About one hundred Bragg reflections could be observed clearly on all detectors. The reflection of 1.58 angstrom in minimum d-spacing which I-obs/sigma(I-obs) > 7 was observed. This result implies that the efficiency of the iBIX will become 50 similar to 100 times higher than that of the present high performance diffracatometer BIX-3 in JAEA after 1MW operation of J-PARC., IOP PUBLISHING LTD
Journal of Physics: Conference Series, 2010年12月, ［査読有り］

A preliminary neutron diffraction analysis of Achromobacter protease I
Yuki Ohnishi; Takeharu Masaki; Taro Yamada; Kazuo Kurihara; Ichiro Tanaka; Nobuo Niimura, Achromobacter protease I (API, E. C. 3.4.21.50) is one of the serine proteases produced by Achromobacter lyticus M497-1. API is distinct from the other tripsin type protease in its lysine specificity. The neutron structure analysis of catalytic triad with Trp169 and His210 was presented. His57 was double protonated and formed hydrogen bonds to Ser194O(gamma) and Asp113O(delta 1), O-delta 2., IOP PUBLISHING LTD
Journal of Physics: Conference Series, 2010年12月, ［査読有り］

A preliminary neutron crystallography on the trypsin-bovine pancreatic trypsin inhibitor complex
K. Kawamura; T. Yamada; K. Kurihara; T. Tamada; R. Kuroki; I. Tanaka; N. Niimura, Trypsin is one of serine proteases. BPTI (Bovine Pancreatic Trypsin Inhibitor) is a protein inhibitor, which binds trypsin tightly and inhibits cleavage of peptide bonds. X-ray structure determination of trypsin-BPTI complex could make clear the overview of the active site. However, information of hydrogen atoms related to catalytic mechanism has not been satisfied. In this study, the trypsin-BPTI complex structure has been determined by neutron diffraction data at 2.0 angstrom resolution. Deuterium atoms of catalytic triad, hydration structures in the binding pocket of trypsin and hydrogen bonds were observed. We would like to discuss details of hydrogen bonds in the interface between trypsin and BPTI and the adjacent water molecules including hydrogen atoms involved in the enzymatic reaction., IOP PUBLISHING LTD
Journal of Physics: Conference Series, 2010年12月, ［査読有り］

Neutron Structure Analysis by IBARAKI Biological Crystal Diffractometer (iBIX) in J-PARC　　　　　　　　　　　　　　　
Ichiro Tanaka; Katsuhiro Kusaka; Takaaki Hosoya; Nobuo Niimura; Takashi Ohhara; Kazuo Kurihara; Taro Yamada; Yuki Ohnishi; Katsuaki Tomoyoria; Takeshi Yokoyama
Acta Cryst. D, 2010年09月, ［査読有り］, ［招待有り］

[Beginning of use of a new biological neutron diffractometer (iBIX) in J-PARC].
Tanaka I; Kusaka K; Hosoya T; Ohhara T; Kurihara K; Niimura N
Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan, 2010年05月, ［査読有り］

Anomalous Water Molecules and Mechanistic Effects of Water Nanotube Clusters Confined to Molecular Porous Crystals
Makoto Tadokoro; Takashi Ohhara; Yuhki Ohhata; Takaaki Suda; Yuji Miyasato; Takeshi Yamada; Tatsuya Kikuchi; Ichiro Tanaka; Kazuo Kurihara; Masaharu Oguni; Kazuhiro Nakasuji; Osamu Yamamuro; Kuroki Ryota, The movement of water molecules in the limited space present within nanoscale regions, which is different from the molecular motion of bulk water, is significantly affected by strong interfacial interactions with the surrounding outer walls. Hence, most of the water molecules that are confined to nanochannel spaces having widths less than ca. 2 nm can generally be classified together as "structural water". Since the motions of such water molecules are limited by interfacial interactions with the outer wall, the nature of structural water, which is strongly influenced by the interactions, will have different characteristics from normal water. For our investigations on the characteristics of structural water, we have developed a nanoporous crystal with a diameter of ca. 1.6 nm; it was constructed from 1-D hydrophilic channels by self-organization of the designed molecules. A tubelike three-layered water cluster, called a water nanotube (WNT), is formed in each internal channel space and is regulated by H-bonds with the outer wall. The WNT undergoes a glass transition (T-g = 107 K) and behaves as a liquid; it freezes at 234 K and changes into an icelike nanotube cluster. In this study, the structure of the WNT is investigated through neutron structure analysis, and it is observed to stabilize by a mechanistic anchor effect of structural water. Furthermore, from neutron-scattering experiments, it is seen that a few water molecules around the center of the WNT move approximately with the same diffusion constant as those in bulk water; however, the residence time and average jump length are longer, despite the restrictions imposed by the H-bonding with structural water. The behavior of mobile water within a WNT is investigated; this can be used to elucidate the mechanism for the effect of structural water on vital functions on the cell surface., AMER CHEMICAL SOC
JOURNAL OF PHYSICAL CHEMISTRY B, 2010年02月, ［査読有り］

2P025 変異体トランスサイレチンの中性子回折測定及びX線結晶構造解析(蛋白質-構造,第48回日本生物物理学会年会)
Yokoyama Takeshi; Nabeshima Yuko; Hosoya Takaaki; Ohara Takashi; Kurihara Kazuo; Kusaka Katsuhiro; Mizuguchi Mineyuki; Tanaka Ichiro; Niimura Nobuo, 一般社団法人 日本生物物理学会
生物物理, 2010年

BL03茨城県生命物質構造解析装置(iBIX)
田中伊知朗; 田中伊知朗; 日下勝弘; 細谷孝明; 大原高志; 栗原和男; 新村信雄, 茨城県生命物質構造解析装置iBIXでの初めてのタンパク質測定等の報告および結晶体積および加速器出力の関数としての測定条件の概算, 日本中性子科学会
日本中性子科学会誌｢波紋｣, 2010年01月, ［招待有り］

供用を開始したJ-PARCの新しい生物用中性子回折装置(iBIX)
田中伊知朗; 日下勝弘,細谷孝明; 大原高志; 栗原和男; 新村信雄, Ibaraki Prefectural Government together with Ibaraki University and Japan Atomic Energy Agency (JAEA) has almost finished constructing a time-of-flight (TOF) neutron diffractometer for biological macromolecules for industrial use at J-PARC, IBARAKI Biological Crystal Diffractometer (iBIX). Since 2009, Ibaraki University has been asked to operate this machine in order for users to do experiments by Ibaraki Prefecture. The diffractometer is designed to cover sample crystals which have their cell edges up to around 150 Å. It is expected to measure more than 100 samples per year if they have 2 mm³ in crystal volume, and to measure even around 0.1 mm³ in crystal volume of biological samples. The efficiency of iBIX is also expected about 100 times larger than those of the present high performance diffractometers at JRR-3 in JAEA when 1MW power realizes in J-PARC. Since December 2008, iBIX has been open to users and several proteins and organic compounds were tested under 20 kW proton power of J-PARC. It was found that one of their proteins was diffracted up to 1.4 Å in d-spacing, which was nearly comparable resolution to that of BIX-3 in JRR-3 when used the same crystal as at iBIX for reasonable exposure time. In May 2009, 14 detector units were set up. By the end of fiscal year 2009, the basic part of data reduction software will be finished and an equipment blowing low temperature gas to the sample will be installed with the cooperation of JAEA.
, 公益社団法人 日本薬学会
薬学雑誌, 2010年, ［査読有り］, ［招待有り］

A neutron crystallographic analysis of T6 porcine insuline at 2.1 A resolution
W. Iwai; T. Yamada; K. Kurihara; Y. Ohnishi; Y. Kobayashi; I. Tanaka; H. Takahashi; R. Kuroki; T. Tamada; N. Niimura, Neutron diffraction data for T6 porcine insulin were collected to 2.1 Å resolution from a single crystal partly deuterated by exchange of mother liquor. A maximum-likelihood structure refinement was undertaken using the neutron data and the structure was refined to a residual of 0.179. The hydrogen-bonding network of the central core of the hexamer was observed and the charge balance between positively charged Zn ions and their surrounding structure was interpreted by considering the protonation and/or deprotonation states and interactions of HisB10, water and GluB13. The observed double conformation of GluB13 was essential to interpreting the charge balance and could be compared with the structure of a dried crystal of T6 human insulin at 100 K. Differences in the dynamic behaviour of the water molecules coordinating the upper and lower Zn ions were observed and interpreted. The hydrogen bonds in the insulin molecules, as well as those involving HisB10 and GluB13, are discussed. The hydrogen/deuterium (H/D) exchange ratios of the amide H atoms of T6 porcine insulin in crystals were obtained and showed that regions highly protected from H/D exchange are concentrated in the centre of a helical region of the B chains. From the viewpoint of soaking time versus H/D-exchange ratios, the amide H atoms can be classified into three categories. © 2009 International Union of Crystallography.
Acta Cryst. D, 2009年09月, ［査読有り］

A neutron crystallographic analysis of phosphate-free ribonuclease A at 1.7 A resolution
D. Yagi; T. Yamada; K. Kurihara; Y. Ohnishi; M. Yamashita; T. Tamada; I. Tanaka; R. Kuroki and N. Niimura, A neutron crystallographic analysis of phosphate-free bovine pancreatic RNase A has been carried out at 1.7 Å resolution using the BIX-4 single-crystal diffractometer at the JRR-3 reactor of the Japan Atomic Energy Agency. The high-resolution structural model allowed us to determine that His12 acts mainly as a general base in the catalytic process of RNase A. Numerous other distinctive structural features such as the hydrogen positions of methyl groups, hydroxyl groups, prolines, asparagines and glutamines were also determined at 1.7 Å resolution. The protonation and deprotonation states of all of the charged amino-acid residues allowed us to provide a definitive description of the hydrogen-bonding network around the active site and the H atoms of the key His48 residue. Differences in hydrogen-bond strengths for the - helices and Β-sheets were inferred from determination of the hydrogen-bond lengths and the H/D-exchange ratios of the backbone amide H atoms. The correlation between the B factors and hydrogen-bond lengths of the hydration water molecules was also determined. © 2009 International Union of Crystallography.
Acta Cryst. D, 2009年08月, ［査読有り］

生物用単結晶構造解析装置　　　　　　　　　　　　　　　
田中伊知朗
日本金属学会誌｢まてりあ｣, 2009年07月, ［査読有り］

Methyl group conformation and hydrogen bonds in proteins determined by neutron protein crystallography
Atsushi Yamaguchi; Kouji Shibata; Ichiro Tanaka; Nobuo Niimura, Using 'Hydrogen and Hydration in Proteins Data Base' (HHDB) that catalogs all H atom positions in biological macromolecules and in hydration water molecules that have been determined thus far by neutron macromolecular crystallography, methyl group conformation and hydrogen bonds (H.B.) in proteins are explored. It is found that most of the methyl groups belong to the stable staggered conformation but 11% of them seemed to be close to the eclipsed conformation. And geometrical consideration has been done for H.B. involved in a-helices. 125 H.B. were identified as donors for acceptor C=O in the main chain alpha-helix. For these H.B., it is found that co-linear H.B. were rare, that hydrogen atoms seen from acceptors C=O can localize upon certain arrangements, that H.B. are not parallel to the helix axis but rather inclined to C-terminal direction, and that hydrogen atoms except water are located inside, not outside of cylinders which the backbones of alpha-helices form. (C) 2009 Published by Elsevier B.V., ELSEVIER SCIENCE BV
Nucl. Instr. Meth. A, 2009年02月, ［査読有り］

Overview of a New Biological Neutron Diffractometer (iBIX) in J-PARC
Ichiro Tanaka; Katsuhiro Kusaka; Katsuaki Tomoyori; Nobuo Niimura; Takashi Ohhara; Kazuo Kurihara; Takaaki Hosoya; Tomoji Ozeki, Since 2004, Ibaraki Prefectural Government in Japan has started to construct a Time-of-Flight (TOF) neutron diffractometer for biological macromolecules for industrial use at J-PARC, near JRR-3 in JAEA. From 2008, Ibaraki University will operate this machine with the support of Ibaraki Prefecture in order for users to do experiments. The diffractometer is designed so that it can measure crystals the maximum cell dimension of which is up to around 160 angstrom. It is expected to measure more than 100 samples per year if they have 2 mm(3) in crystal volume. As a result, the efficiency will be more than 100 times higher than that of the present high performance diffractometer, BIX-4 in JRR-3 reactor in JAEA. To realize this performance, a coupled moderator (intense neutrons, but broad pulse in time resolution) was selected. In addition, two important and key items should be developed: a new detector with high spatial resolution (less than I mm) and a special program to de-convolute overlapped Bragg reflections on the raw data. The detector uses ZnS:Ag(6)/LiF scintillator with wavelength-shift-fiber (WLSF) system. The program has been designed using a complicated kind of profile-fitting method. The current status of these developments as well as the diffractometer constructions is reported. (C) 2008 Published by Elsevier B.V., ELSEVIER SCIENCE BV
Nucl. Instr. Meth. A, 2009年02月, ［査読有り］

Development of data processing software for a new TOF single crystal neutron diffractometer at J-PARC
T. Ohhara; K. Kusaka; T. Hosoya; K. Kurihara; K. Tomoyori; N. Niimura; Ichiro Tanaka; J. Suzuki; T. Nakatani; T. Otomo; S. Matsuoka; K. Tomita; Y. Nishimaki; T. Ajima; S. Ryufuku, We have developed new data processing software for a new time-of-flight (TOF) single crystal neutron diffractometer at the Materials and Life-science Facility (MLF) of the Japan Proton Accelerator Research Complex (J-PARC); IBARAKI Biomolecular Crystal Diffractometer (iBIX). This software, named "STARGazer", makes a HKLF list from three-dimensional (x, y, TOF) raw data of the iBIX. The STARGazer has both a data processing part and a data visualization part. The former part is a main part to make a HKLF list. This part has fundamental data processing functions and additional functions, real-space indexing, refinement of detector positions simultaneously with an UB matrix, and finding overlapping Bragg reflections, to process diffraction data of bio-macromolecular crystal which has large unit cell volumes. The latter part displays the three-dimensional raw data with predicted positions of Bragg reflections to confirm how well an obtained UB matrix fits to the raw data. In the near future, a function to process overlapping Bragg reflections based on a profile fitting technique will be added to the STARGazer. (c) 2008 Elsevier B.V. All rights reserved., ELSEVIER SCIENCE BV
Nucl. Instr. Meth. A, 2009年02月, ［査読有り］

Construction of Ibaraki Prefectural neutron spectrometers
M. Hayashi; T. Ishigaki; T. Kamiyama; Ichiro Tanaka, Ibaraki Prefectural Government established Science Frontier 21 Initiative (SF21) in 2001. In SF21 the active co-operations between Tsukuba, Tokai and Hitachi areas are accelerated and two Prefecture's neutron spectrometers have been constructed in order to establish the advanced industrial zone by setting the J-PARC as a key component. In addition, the industrial applications of neutron will be promoted. The objectives of SF21 are promotion of industrial applications of J-PARC, grow-up of neutron research scientists, and establishment of infrastructure supporting international collaboration. In this paper, outline of the two Ibaraki prefecture's spectrometers are described. (C) 2008 Elsevier B.V. All rights reserved., ELSEVIER SCIENCE BV
Nucl. Instr. Meth. A, 2009年02月, ［査読有り］

Abnormal pKa value of internal histidine of the insulin molecule revealed by neutron crystallographic analysis　　　　　　　　　　　　　　　
Takuya Ishikawa; Toshiyuki Chatake; Yukio Morimoto; Mitsuru Maeda; Kazuo Kurihara; Ichiro Tanaka; Nobuo Niimura
Biochem. Biophys. Res. Comm., 2008年09月, ［査読有り］

Hydrogen Bonds of DsrD Protein Revealed by Neutron Crystallography
T. Chatake; Y. Higuchi; N. Mizuno; I. Tanaka; N. Niimura; Y. Morimoto
J. Synchrotron Rad, 2008年05月, ［査読有り］

中性子解析で明らかにされたプロトン化が関わる生体反応
石川卓哉、田中伊知朗、新村信雄, Protonation is the key to elucidate a function of protein.Neutron crystallographic analysis is a powerful method that can observe the protonation states of amino acid residues in a protein molecule. However the neutron crystallographic technique was very difficult method, because of low flux neutron source mainly. Recently, a neutron imaging plate and an elastically bent perfect Si monochromator enabled neutron experiment. As the result, neutron structural biology has been progressed greatly in these ten years. In this report, we explain the various biological reactions affected by the protonation state on protein molecules by our studies on neutron crystallographic analysis. Furthermore, we also introduce our recent study on the protonation of cubic insulin molecule., The Japanese Society for Neutron Science
日本中性子科学会誌｢波紋｣, 2008年04月, ［査読有り］

A neutron crystallographic analysis of a cubic porcine insulin at pD6.6
Takuya Ishikawa; Toshiyuki Chatake; Yuki Ohnishi; Ichiro Tanaka; Kazuo Kurihara; Ryota Kuroki; Nobuo Niimura, The pK(a) values of ionizable amino acid side chains are tabulated in standard textbooks. However, whether a certain amino acid side chain in a protein is charged or not cannot be estimated from standard pH values measured from protein solutions. Protonation and deprotonation of various ionizable amino acid residues were observed by a neutron diffraction experiment and discussed on the basis of the charged states estimated by the pK(a) values of the amino acid residues.
The neutron diffraction study has been carried out at 2.7 angstrom resolution on cubic porcine insulin at pD 6.6 using the BIX-4 single crystal diffractometer at the JRR-3 reactor of the Japan Atomic Energy Agency. For the present work, a large single crystal of 2.7 mm 3 (=2.0 x 1.7 x 0.8 mm) was obtained by dialysis. The structure refinement was carried out using the program CNS. The resulting R(cryst) is 21.6% and the R(free) is 29.1% at a resolution of 2.7 angstrom.
In the case of HisB5, both N pi and N tau of an imidazole ring are protonated at pD 6.6, but at pD 9 only N pi is protonated. In contrast, for HisB10, both N pi and N tau are protonated at pD 6.6 as well as at pD 9. The ionization states of several amino acids in porcine insulin have been obtained at pD 6.6 and they are compared with those at pD 9 obtained by neutron diffraction as well as those at pH 6.50 and 6.98 obtained by X-ray diffraction. In this manuscript, the difference between these forms will be discussed. (C) 2007 Elsevier B.V. All rights reserved., ELSEVIER SCIENCE BV
Chemical Physics, 2008年04月, ［査読有り］

New sources and instrumentation for neutrons in biology
S.C.M. Teixeira; G. Zaccai; J. Ankner; M.C. Bellissent-Funel; R. Bewley; M.P. Blakeley; P. Callow; L. Coates; R. Dahint; R. Dalgliesh; N.A. Dencher; V.T. Forsyth; G. Fragneto; B. Frick; R. Gilles; T. Gutberlet; M. Haertlein; T. Hauß; W. Häußler; W.T. Heller; K. Herwig; O. Holderer; F. Juranyi; R. Kampmann; R. Knott; S. Kreuger; P. Langan; R.E. Lechner; G. Lynn; C. Majkrzak; R.P. May; F. Meilleur; Y. Mo; K. Mortensen; D.A.A. Myles; F. Natali; C. Neylon; N. Niimura; J. Ollivier; A. Ostermann; J. Peters; J. Pieper; A. Rühm; D. Schwahn; K. Shibata; A.K. Soper; Th. Straessle; J. Suzuki; I. Tanaka; M. Tehei; P. Timmins; N. Torikai; T. Unruh; V. Urban; R. Vavrin; K. Weiss, Neutron radiation offers significant advantages for the study of biological molecular structure and dynamics. A broad and significant effort towards instrumental and methodological development to facilitate biology experiments at neutron sources worldwide is reviewed. (C) 2008 Elsevier B.V. All rights reserved., ELSEVIER SCIENCE BV
Chemical Physics, 2008年04月, ［査読有り］

Crystallization and evaluation of hen egg-white lysozyme crystals for protein pH titration in the crystalline state
Wakari Iwai; Daichi Yagi; Takuya Ishikawa; Yuki Ohnishi; Ichiro Tanaka; Nobuo Niimura, To observe the ionized status of the amino acid residues in proteins at different pH (protein pH titration in the crystalline state) by neutron diffraction, hen egg-white lysozyme was crystallized over a wide pH range (2.5-8.0). Crystallization phase diagrams at pH 2.5, 6.0 and 7.5 were determined. At pH <
4.5 the border between the metastable region and the nucleation region shifted to the left (lower precipitant concentration) in the phase diagram, and at pH >
4.5 the border shifted to the right (higher precipitant concentration). The qualities of these crystals were characterized using the Wilson plot method. The qualities of all crystals at different pH were more or less equivalent (B-factor values within 25-40). It is expected that neutron diffraction analysis of these crystals of different pH provides equivalent data in quality for discussions of protein pH titration in the crystalline state of hen egg-white lysozyme. © 2008 International Union of Crystallography Printed in Singapore - All rights reserved.
Journal of Synchrotron Radiation, 2008年04月, ［査読有り］

新型生体高分子回折計（iBIX）の概要と化学・生命科学にもたらす新展開　　　　　　　　　　　　　　　
田中伊知朗、日下勝弘、友寄克亮、新村信雄、大原高志、栗原和男、細谷孝明、尾関智二
日本結晶学会誌, 2008年02月, ［査読有り］, ［招待有り］

Preliminary expriment for neutron diffraction study of proteinase K　　　　　　　　　　　　　　　
T. Chatake; T. Ishikawa; A. Kawaguchi; Y. Morimoto; Y. Yanagisawa; I. Tanaka
KURRI Progress Report 2007, 2008年

Structural Refinement and Extraction of hydrogen Atomic Positions in Polyoxymethylene Crystal Based on the First Successful Measurements of 2-Dimensional High-Energy Synchrotron X-ray Diffraction and Wide-Angle Neutron Diffraction Patterns of Hydrogenated and Deuterated Species
Kohji Tashiro; Makoto Hasegawa; Takashi Ohhara; Tomoji Ozeki; Toshiaki Kitano; Takashi Nishu; Kazuo Kurihara; Taro Tamada; Ryota Kuroki; Satoru Fujiwara; Ichiro Tanaka; Nobuo Niimura, 2-Dimensional X-ray and neutron diffraction patterns have been successfully measured for deuterated and hydrogenated polyoxymethylene (POM) samples obtained by gamma-ray induced solid-state polymerization reaction. More than 700 reflections were collected from the X-ray diffraction data at -150 degrees C by utilizing a high-energy synchrotron X-ray beam at SPring-8, Japan, from which the crystal structure of POM has been refined thoroughly including the extraction of hydrogen atomic positions as clearly seen in the difference Fourier synthesis map. As the first trial the nonuniform (9/5) helical model was analyzed with the reliability factor (R factor) 6.9%. The structural analysis was made also using the X-ray reflections of about 400 observed at room temperature (R 8.8%), and the thermal parameters of constituent atoms were compared between the low and high temperatures to discuss the librational thermal motion of the chains. The 2-dimensional neutron diffraction data, collected for the deuterated and hydrogenated POM samples using an imaging plate system specifically built-up for neutron scattering experiment, have allowed us to pick up the D and H atomic positions clearly in the Fourier synthesis maps. Another possible model, (29/16) helix, which was proposed by several researchers, has been also investigated on the basis of the X-ray diffraction data at -150 C. The direct method succeeded in extracting this (29/16) model straightforwardly. The R factor was 8.6%, essentially the same as that of (9/5) helical model. This means that the comparison of the diffraction intensity between the data collected from the full-rotation X-ray diffraction pattern and the intensity calculated for both the (9/5) and (29/16) models cannot be used for the unique determination of the superiority of the model, (9/5) or (29/16) helix. However, we have found the existence of 001 and 002 reflections which give the longer repeating period 55.7 angstrom. Besides there observed a series of meridional 00l reflections forbidden for (9/5) helical model. These additional evidences support the nonuniform (29/16) helical model as the most plausible chain conformation of POM crystal., NATURE PUBLISHING GROUP
Polymer Journal, 2007年12月, ［査読有り］

Protonation States of Buried Histidine Residues in Human Deoxyhemoglobin Revealed by Neutron Crystallography　　　　　　　　　　　　　　　
Toshiyuki Chatake; Naoya Shibayama; Sam-Yong Park; Kazuo Kurihara; Taro Tamada; Ichiro Tanaka; Nobuo Niimura; Ryota Kuroki; Yukio Morimoto
Journal of American Chemical Society (JACS), 2007年11月, ［査読有り］

J-PARCにおける新型生体高分子回折計の建設状況と超高分解能X線解析との相補性について
田中伊知朗, J-PARCに建設中の生体高分子用パルス中性子式回折計の建設状況と水素原子が見えるということで最近注目されている超高分解能X線解析との相補性について述べている。新型回折計は順調に建設が進んでおり、既存の装置の100倍以上の測定効率を期待できる。また、X線ではプロトンは見えないのだから、この点で、十分相補的にデータを解釈することでより新しい生命科学の分野が開く可能性がある。, The Japanese Society for Neutron Science
日本中性子科学会誌｢波紋｣, 2007年01月, ［査読有り］, ［招待有り］

Measurements of small organic molecules on the single crystal neutron diffractmeters for biomolecules at JAERI　　　　　　　　　　　　　　　
T.Ohhara; K.Kurihara; T.Tamada; I.Tanaka; N.Niimura; R.Kuroki, 日本原子力研究所JRR-3に設置されている生体高分子用中性子回折計BIX-3およびBIX-4において、比較的小さな有機化合物の単結晶中性子構造解析における仕様、性能を述べるとともに、いくつかの解析例を紹介する。
Physica B, 2006年12月, ［査読有り］

Peak overlapping and its de-convolution in TOF diffraction data from neutron biological diffractometer in J-PARC
K.Kusaka; T.Ohhara; I.Tanaka; N.Niimura; T.Ozeki; K.Kurihara; K.Aizawa; Y.Morii; M.Arai; K.Ebata; Y.Takan, 次世代中性子源であるJ-PARCにおいて建設中の茨城県生命物質構造解析装置のTOFデータにおいて、検出器生データ上でのピークの重なりの評価と重なったピークの分離を目指した手法を論じた。
Physica B, 2006年12月, ［査読有り］

Hydrogen-bond networks involving protonated bicapped-Keggin tetradecavanadophosphate anions
Setsuko Nakamura; Takuto Yamawaki; Katsuhiro Kusaka; Takuhiro Otsuka; Tomoji Ozeki, Tetraphenylphosphonium salts of protonated tetradecavanadophosphate (PV14) anions, [ (C6H5)(4)P](4)H5PV14O42 center dot 5H(2)O (1) and [ (C6H5)(4)P](2)H7PV14O42 center dot 6H(2)O (2), have been synthesized and their crystal structures have been determined. Compound I crystallizes in triclinic, P1 with a = 12.7866(2), b = 15.5261(2), c = 16.0730(3) angstrom, alpha = 109.358(1), beta = 98.411(1), gamma = 110.040(1)degrees. Synchrotron radiation X-ray diffraction revealed that compound 2 crystallizes in monoclinic, P2(1)/c with a = 16.821(1), b = 25.163(2), c = 18.817(1) angstrom, beta = 109.992(2)degrees. In compound 1, the PV14 anions are linked into a one-dimensional chain structure by water molecules of crystallization. In compound 2, hydrogen bonds directly link PV14 anions into a zigzag chain, which are then woven into a three-dimensional network by hydrogen bonds bridged by water molecules., SPRINGER/PLENUM PUBLISHERS
JOURNAL OF CLUSTER SCIENCE, 2006年06月, ［査読有り］

Neutron Biological Diffractometer in J-PARC Proposed by Ibaraki Prefectural Government　　　　　　　　　　　　　　　
I.Tanaka; N. Niimura; T. Ozeki; T. Ohhara; K. Kurihara; K. Kusaka; Y. Morii; K. Aizawa; M. Arai; T, Kasao; K. Ebata; Y. Takano, J-PARCにおいて茨城県が出資する生体高分子用パルス中性子用回折計の建設が始まり、現在、その詳細設計を行っている。135Åまでの単位格子結晶で2mm角程度の結晶が使用できれば、年間100個程度の構造解析が可能となり、十分産業利用にも供することが期待される。この測定効率は、現存の高性能装置の100倍以上である。
ICANS-XVII Proceedings, LA-UR-3904, 2006年06月, ［招待有り］

Recent results on hydrogen and hydration in biology studied by neutron macromolecular crystallography　　　　　　　　　　　　　　　
Nobuo Niimura; Shigeki Arai; Kazuo Kurihara; Toshiyuki Chatake; Ichiro Tanaka; Robert Bau
Cellular and Molecular Life Sciences, 2006年02月, ［査読有り］

Direct Observation of Deuterium Transfer in Crystalline-State Chiral Thiolactam Formation by Neutron Diffraction Analysis　　　　　　　　　　　　　　　
Takaaki Hosoya; Hidehiro Uekusa; Yuji Ohashi; Takashi Ohhara; Ichiro Tanaka; Nobuo Niimura
Acta Crystallographica Section B, 2006年, ［査読有り］

Neutron diffraction analysis of deuterium transfer in chiral β-thiolactam formation in the crystalline state
Takaaki Hosoya; Hidehiro Uesaka; Yuji Ohashi; Takashi Ohhara; Ichiro Tanaka; Nobuo Niimura
Acta Crystallographica B, 2006年01月, ［査読有り］

Neutron Crystallographic Analysis Of The Z-DNA Hexamer CGCGCG　　　　　　　　　　　　　　　
T. Chatake; I. Tanaka; H. Umino; S. Arai; N. Niimura
Acta Cryst. D, 2005年06月

Complicated Water Orientations in the minor groove of B-DNA decamer d(CCATTAATGG)2 observed by Neutron Diffraction Measurements
Arai S.; Chatake T.; Ohhara T.; Kurihara K.; Tanaka I.; Suzuki N.; Fujimoto Z.; Mizuno H. and Niimura N., It has long been suspected that the structure and function of a DNA duplex can be strongly dependent on its degree of hydration. By neutron diffraction experiments, we have succeeded in determining most of the hydrogen ( H) and deuterium ( D) atomic positions in the decameric d( CCATTAATGG)(2) duplex. Moreover, the D positions in 27 D2O molecules have been determined. In particular, the complex water network in the minor groove has been observed in detail. By a combined structural analysis using 2.0 &ANGS; resolution X-ray and 3.0 &ANGS; resolution neutron data, it is clear that the spine of hydration is built up, not only by a simple hexagonal hydration pattern ( as reported in earlier X-ray studies), but also by many other water bridges hydrogen- bonded to the DNA strands. The complexity of the hydration pattern in the minor groove is derived from an extraordinary variety of orientations displayed by the water molecules., OXFORD UNIV PRESS
Nucleic Acids Res., 2005年05月

Single Crystal Pulsed Neutron Diffractometer for Biologically Important Materials Crystallography No.1 (BIX-P1) at Material and Life Science Facility in J-PARC
I.TANAKA; T.OZEKI; T.OHHARA; K.KURIHARA; N.NIIMURA, Japan proton accelerator research complex (J-PARC) with the power of 1MW have been constructing since 2001 in JAERI, Japan. And the first beam will come by 2007. As one important day-one neutron instruments at Material and Life Science Facility in J-PARC, a single crystal diffractometer No.1 for structural analysis of biological macromolecules and organic compounds with unit cell dimensions less than about 135Å (BIX-P1) has been proposed, considering the international competition in biological science and the expansion of the application to the industrial fields. It is expected to gain efficiency more than 50 times larger than neutron biological diffractometers BIX-3 and BIX-4 installed at JRR-3 reactor also in JAERI. In this paper, evaluation of moderator, items of necessary R &
D and the current specification of BIX-P1 are shown. © 2004 Taylor &
Francis Ltd.
Journal of Neutron Research, 2005年02月, ［招待有り］

Endohedral Clusterization of Ten Water Molecules into a "Molecular Ice" within the Hydrophobic Pocket of a Self-Assembled Cage
Yoshizawa; M.; Kusukawa; T.;; Kawano; M.; Ohhara; T.; Tanaka; I.; Kurihara; K.; Niimura; N.; Fujita; M., AMER CHEMICAL SOC
J. Am. Chem. Soc., 2005年

Neutron crystallographic study on rubredoxin from Pyrocuccus furiosus by BIX-3, a single-crystal diffractometer for biomacromolecules
K. Kurihara; I. Tanaka; T. Chatake; M. W. W. Adams; F. E. Jenny Jr.; N. Moiseeva; R. Bau; N. Niimura, The structure of a partially deuterated rubredoxin from the hyperthermophilic archaeon Pyrococcus furiosus, an organism that grows optimally at 100degreesC, was determined by using the neutron single-crystal diffractometer dedicated for biological macromolecules (BIX-3) at the JRR-3M reactor of the Japan Atomic Energy Research Institute. Data were collected at room temperature up to a resolution of 1.5 Angstrom, and the completeness factor of the data set was 81.9%. The model contains 306 H and 50 D atoms. A total of 37 hydration water molecules were identified, with 15 having all three atoms fully located and the remaining D2O molecules partially defined. The model has been refined to final agreement factors of R = 18.6% and R-free = 21.7%. Several orientations of the O-D bonds of side chains, whose assignments from x-ray data were previously ambiguous, were clearly visible in the neutron structure. Although most backbone N-H bonds had undergone some degree of H/D exchange throughout the rubredoxin molecule, 5 H atom positions still had distinctly negative (H) peaks. The neutron Fourier maps clearly showed the details of an extensive set of H bonds involving the ND3+ terminus that may contribute to the unusual thermostability of this molecule., NATL ACAD SCIENCES
Proc. Natl. Acad. Sci. USA, 2004年08月

Neutron Protein Crystallography in JAERI
I. Tanaka, Neutron diffraction provides an experimental method of directly locating hydrogen atoms in proteins. After developing an original neutron detector (neutron imaging plate) and a novel practical neutron monochromator (elastically bent perfect Si monochromator), BIX-type diffractometers which were equipped with these tools were efficiently constructed at JRR-3 in Japan Atomic Energy Research Institute (JAERI), Japan and they have finished many protein crystallographic measurements and interesting results have come one after another. At the same time a method of growing large protein single crystals and a database of hydrogen and hydration have also been developed. In the near future, a pulsed neutron diffractometer for biological macromolecules has been proposed at J-PARC in JAERI., INDIAN ACADEMY SCIENCES
Pramana-J. Phys., 2004年07月, ［招待有り］

中性子科学への招待（３）－中性子単結晶構造解析、生物回折計
栗原和男、田中伊知朗、新村信雄, Neutron diffraction provides an experimental method of directly locating hydrogen atoms in proteins and nucleic acids, and the development of the neutron imaging plate (NIP) became a breakthrough event in neutron protein crystallography. A high resolution neutron diffractometers dedicated to biological macromolecules (BIX-3, BIX-4) with the NIP have been constructed at Japan Atomic Energy Research Institute. The detailed structure of the diffractometer and the systematic procedure of the neutron diffraction experiment from the crystallization of a large single crystal to the data collection and the data processing, and the future prospect of the neutron diffractometry in proteins will be presented., The Crystallographic Society of Japan
日本結晶学会誌, 2004年06月, ［招待有り］

イメージングプレートを利用した合成高分子の2次元中性子回折像測定ならびに水素原子位置の抽出：中性子、X線、電子線構造解析結果を比較して
田代孝二、田中伊知朗、大原高志、新村信雄、藤原悟、栗原和男、釜江俊也, 2-Dimensional wide-angle neutron diffraction patterns have been measured successfullyfor the uniaxially-oriented samples of fully-deuterated and fully-hydrogeneouspolyethylene by using BIX-3 imaging plate system installed at the Japan Atomic Energy Research Institute.These data were analyzed in detail and the calculation of Fouriermaps allowed us to extract the positions of hydrogen atoms in the crystal latticeaccurately.The structural parameters obtained after refinement were compared withthose derived from the X-ray and electron diffraction experiments as well as thecomputer simulation result. The accurate determination of hydrogen atomic position byneutron technique makes it possible to perform the exact prediction of physicalproperties of polymer crystals in a quantitative manner., The Japanese Society for Neutron Science
日本中性子科学会誌｢波紋｣, 2004年04月

Hydration structures in proteins and neutron diffraction experiment on dissimilatory sulfite reductase D (DsrD)
T. Chatake; A. Ostermann; K. Kurihara; F. G. Parak; N. Mizuno; G. Voordouw; Y. Higuchi; I. Tanaka; N. Niimura, Neutron crystallography can provide a substantial amount of information about the hydration of proteins. The hydration patterns of three proteins, whose structures have been solved at 1.5 or 1.6 Angstrom resolution using our BIX-type diffractometers, show interesting features. The water molecules adopt a variety of shapes in the neutron Fourier maps, revealing details of intermolecular hydrogen-bond formation and dynamics of hydration. In addition, the neutron diffraction study of a DNA-binding protein, dissimilatory sulfite reductase D (DsrD) is briefly described, and some preliminary results are presented. This topic is of interest because it is well-known that hydrogen bonds play important roles in DNA-protein recognition., BLACKWELL MUNKSGAARD
J. Synchr. Rad., 2004年01月, ［招待有り］

A new neutron single crystal diffractometer dedicated for biological macromolecules (BIX-4)
K. Kurihara; I. Tanaka; M. Refai-Muslih; A. Ostermann and N. Niimur, We have constructed a new neutron single crystal diffractometer (BIX-4) at 1G-B port of JRR-3M in JAERI. Since at 1G-B port another diffractometer for biology, BIX-3 and a high-resolution powder diffractometer (HR-PD) coexist, the monochromator house needed to be reconstructed. The main architecture of BIX-4 is based on that of BIX-3. BIX-4 uses an elastically-bent perfect-Si crystal monochromator and neutron imaging plates as BIX-3. In addition, several optimizations of the monochromator and modifications from previous BIX-3 are carried out. The final gain of the neutron intensity at the detector position is estimated to be 2.5 times larger than previous BIX-3. That higher performance increases the opportunities to apply neutron crystallography to biological macromolecules which give only weak reflections and/or small crystals., BLACKWELL MUNKSGAARD
J. Synchr. Rad., 2004年01月

Crystallization of a large single crystal of cubic insulin for neutron protein crystallography
M. Maeda; T. Chatake; I. Tanaka; A. Ostermann and N. Niimura, The growth of a large single crystal of cubic porcine insulin for characterization of hydrogen and hydration in cubic insulin crystals by neutron diffraction analysis is reported. Growth in D2O was investigated based on the phase diagram for cubic insulin to determine appropriate growth conditions, and a large single crystal was then successfully grown by a dialysis method to a size of 4.0 x 4.0 x 1.3 mm(3). Neutron diffraction analysis of the cubic insulin crystals was carried out using a single-crystal diffractometer at the JRR-3M reactor of the Japan Atomic Energy Research Institute. In preliminary analysis, N-pi. appears to be protonated and N-tau, deprotonated in His5 in the B-chain, whereas both N-pi. and N-tau, are protonated in His10., BLACKWELL MUNKSGAARD
J. Synchr. Rad., 2004年01月

Extraction of Hydrogen-Atom Positions in Polyethylene Crystal Lattice from Wide-Angle Neutron Diffraction Data Collected by a Two-Dimensional Imaging Plate System: Comparison with the X-ray and Electron Diffraction Results
K. Tashiro; I. Tanaka; T. Oohara; N. Niimura; S. Fujiwara and T. Kamae, Two-dimensional wide-angle neutron diffraction patterns have been measured successfully for uniaxially oriented fully deuterated and fully hydrogeneous polyethylene samples by using an imaging plate system (BIX-3) installed at the Japan Atomic Energy Research Institute. The detailed data analysis allowed us to extract the positions of hydrogen atoms in the crystal lattice accurately. The results were compared quantitatively with those obtained from the X-ray and electron diffraction experiments as well as the computer simulation result., AMER CHEMICAL SOC
Macromolecules, 2004年

A neutron crystallographic analysis of a rubredoxin mutant at 1.6 A resolution
Toshiyuki Chatake; Kazuo Kurihara; Ichiro Tanaka; Irina Tsyba; Robert Bau; Francis E. Jenney Jr.; Michael W. W. Adams and Nobuo Niimura, A neutron diffraction study has been carried out at 1.6 Angstrom resolution on a mutant rubredoxin from Pyrococcus furiosus using the BIX-3 single-crystal diffractometer at the JRR-3 reactor of the Japan Atomic Energy Research Institute. In order to study the unusual thermostability of rubredoxin from P. furiosus ( an organism that grows optimally at 373 K), the hydrogen-bonding patterns were compared between the wild-type protein and a 'triple-mutant' variant. In this mutant protein, three residues were changed (Trp3 --> Tyr3, Ile23 --> Val23, Leu32 --> Ile32) so that they are identical to those in a mesophilic rubredoxin from Clostridium pasteurianum. In the present study, some minor changes were found between the wild-type and mutant proteins in the hydrogen-bonding patterns of the Trp3/Tyr3 region. In this investigation, the H/D-exchange ratios in the protein were also studied. Because the target protein was soaked in D2O during the crystallization procedure, most of the N - H and O - H bonds have become deuterated, while essentially all of the C - H bonds have not. In particular, the H/D-exchange pattern of the N - H amide bonds of the protein backbone is of interest because it may contain some indirect information about the mechanism of unfolding of this small protein. The results are in broad agreement with those from solution NMR studies, which suggest that the backbone amide bonds near the four Cys residues of the FeS4 redox center are most resistant to H/D exchange. Finally, the detailed geometries of the water molecules of hydration around the rubredoxin molecule are also reported. The 1.6 A resolution of the present neutron structure determination has revealed a more detailed picture than previously available of some portions of the water structure, including ordered and disordered O - D bonds. Crystallographic details: space group P2(1)2(1)2(1) (orthorhombic), unit-cell parameters a = 34.48, b = 35.70, c = 43.16 Angstrom; final agreement factors R = 0.196 and R-free = 0.230 for 19 384 observed and 6548 unique neutron reflections collected at room temperature; crystal size 4 mm(3); a total of 423 non-H atoms, 290 H atoms and 88 D atoms were located in this study., BLACKWELL MUNKSGAARD
Acta Cryst. D, 2004年

Crystallization and preliminary neutron analysis of the dissimilatopry sulfite reductase D (DsrD) protein from the sulfate-reducing bacterium Desulfovibrio vulgaris
T. Chatake; N. Mizuno; G. Voordouw; Y. Higichi; S. Arai; I. Tanaka; N. Niimura, Dissimilatory sulfite reductase D (DsrD) from Desulfovibrio vulgaris has been crystallized for a neutron diffraction study. The initial crystals obtained were too small for the neutron experiment. In order to obtain a larger crystal (> 1 mm(3)), a combination of two techniques was developed to determine the optimum crystallization conditions: a crystallization phase diagram was obtained, followed by crystal-quality assessment via X-ray diffraction. Using conditions determined in this manner, a large single crystal (1.7 mm(3)) of DsrD protein was subsequently grown in D2O solution by the macroseeding technique. A neutron diffraction experiment was carried out using the BIX-3 diffractometer at the Japan Atomic Energy Research Institute (JAERI), collecting data to 2.4 Angstrom resolution from an optimized crystal., BLACKWELL MUNKSGAARD
Acta Cryst. D, 2003年12月

Single Crystal Neutron Diffractometer for Biologically Important Materials Crystallography (BIX-P1)　　　　　　　　　　　　　　　
I.Tanaka; T. Ozeki; T. Ohhara; K. Kurihara; N. Niimura
ESS 03-136-M1, 2003年09月

High Resolution Neutron Protein Crystallography. Hydrogen and Hydration in Proteins
N. Niimura; T. Chatake; A. Ostermann; K. Kurihara and I. Tanaka, Neutron diffraction provides an experimental method of directly locating hydrogen atoms in proteins, and the development of the neutron imaging plate (NIP) became a breakthrough event in neutron protein crystallography. The general features of the NIP are reviewed. A high resolution neutron diffractometer dedicated to biological macromolecules (BIX-3) with the NIP has been constructed at Japan Atomic Energy Research Institute and this has enabled 1.5 Angstrom resolution structural analyses of several proteins to be carried out. The specifications of BIX-3 and LADI (a quasi-Laue type diffractometer installed in the Institut Laue-Langevin) are compared. The crystal structures of myoglobin, wild type rubredoxin and a mutant of rubredoxin have been carried out using BIX-3. From these studies, several topics, such as the location of hydrogen bonds and certain acidic hydrogen atoms, the identification of methyl hydrogen atoms, details of H/D exchange and dynamical behavior of hydration structures have been investigated, and important information has been extracted from the structural results. Finally, a systematic procedure to grow large single crystals of proteins or nucleic acids is described., R OLDENBOURG VERLAG
Zeitschift Fur Kristallographie, 2003年02月, ［招待有り］

Strategy and Performance of instrument suite for JSNS, J-PARC　　　　　　　　　　　　　　　
M. Arai; I. Tanaka
ESS 03-136-M1, 2003年

Direct observation of deuterium migration in crystalline-state reaction by single crystal neutron diffraction IV. "Hula-twist" rotation of a long alkyl radical produced by photoirradiation.
Ohhara T; Ikeda S; Imura H; Uekusa H; Ohashi Y; Tanaka I; Niimura N
Journal of the American Chemical Society, 2002年12月, ［査読有り］

Neutron Diffraction Experiments of Fully Deuterated B-DNA Crystal　　　　　　　　　　　　　　　
Neutron Diffraction; Experiments of Fully; Deuterated; B-DNA Crystal
JAERI-Review, 2002年

Crystal structure analysis of a hexatungstate by a high-energy X-ray diffraction experiment using an imaging plate Weissenberg camera at the BL04B2 beamline of SPring-8¹
Tomoji Ozeki; Katsuhiro Kusaka; Noritaka Honma; Yuji Nakamura; Setsuko Nakamura; Shunsuke Oike; Nobuhiro Yasuda; Hiroyuki Imura; Hidehiro Uekusa; Maiko Isshiki; Chuji Katayama; Yuji Ohashi, An imaging plate Weissenberg camera was installed in the BL04B2 beamline of SPring-8 aiming at automated crystal structure determinations of small molecules. Since this beamline is designed to provide X-rays with the energies higher than 37 keV (λ < 0.33 Å), this camera is advantageous in crystal structure analyses of heavily X-ray absorbing materials. The title crystal structure analysis led to precise positional parameters and well-behaved displacement parameters not only for heavy atoms but also for light atoms.
Chemistry Letters, 2001年, ［査読有り］

Application of a stacked elastically bent perfect Si monochromator with identical and different crystallographic planes for single crystal and powder neutron diffractometry
Tanaka, I; FU Ahmed; N Niimura, In order to obtain more neutrons at the sample position, two Si(1 1 1) plates of W250 x H40 x T5 mm(3) were stacked and currently succeeded in increasing the flux at the sample position of BIX-III diffractometer with JRR-3M at JAERI, Japan by a factor of 1.6 compared to that of a single Si plate. To improve the data taking efficiency, preliminarily, a multi-wavelength monochromator system of stacked elastically bent perfect Si(1 1 1) and Si(2 2 0) crystals was employed to carry out diffraction experiments of Si powder and a relatively complex single crystal, piperidine cobaloxime. Two wavelengths, lambda(1) = 1.80 Angstrom for Si(2 2 0) and lambda(2) = 2.94 Angstrom for Si(1 1 1) were selected for this experiment. All reflections were collected by a neutron imaging plate detector, and the profiles were found to be symmetric and well defined Gaussians. (C) 2000 Elsevier Science B.V. All rights reserved., ELSEVIER SCIENCE BV
PHYSICA B, 2000年06月, ［査読有り］

3C0945 ルブレドキシンの中性子構造解析
栗原 和男; 田中 伊知朗; Adams M.W.W.; Moiseeva N.; Bau R.; 新村 信雄, 一般社団法人 日本生物物理学会
生物物理, 2000年

An Upgraded Neutron Diffractometer (BIX-III) for Macromolecules with a Neutron Imaging Plate.　　　　　　　　　　　　　　　
An Upgraded Neutron Diffractometer; BIX-III) for Macromolecules with; a Neutron Imaging Plate
JAERI-Review, 2000年

A Neutron Diffractmeter for Biological Maromolecules using Imaging Plates.
米澤康滋
Physica B, 1998年05月, ［査読有り］

(2-Cyano-2, 2-dideuterioethyl) [bis (dimethylglyoximato) ] [N-(2-hydroxyethyl) isonicotinamide] cobalt (III) における結晶相β-α異性化反応の単結晶中性子回折を用いた解析
伊村 宏之; 竹内 和洋; 大原 高志; 大橋 裕二; 田中 伊知朗; 熊沢 紳太郎; 新村 信雄, The Crystallographic Society of Japan
日本結晶学会誌, 1998年

A neutron diffractometer for biological macromolecules using neutron imaging plates
S Fujiwara; Y Karasawa; Tanaka, I; Y Minezaki; Y Yonezawa; N Niimura, Neutron imaging plates (NIPs), developed recently, have a good spatial resolution and availability of a large sensitive area. The NIPs having such characteristics may be particularly useful for neutron-diffraction measurements of biological macromolecules. We have constructed a neutron diffractometer dedicated to crystallography of biological macro-molecules using the NIP, in the guide hall of the reactor JRR-3M at Japan Atomic Energy Research Institute. Neutrons are monochromatized with an elastically-bent-silicon monochromator (lambda = 0.22 nm). The diffraction patterns are detected with the NIP of 400 x 520 mm(2) at a distance of 150-300 mm from a sample crystal. A sequence of the measurements (exposure, reading the NIP, erasure of the pattern, and starting the next exposure) is done automatically. We measured the diffraction patterns from hen egg-white lysozyme crystals, and obtained the patterns which can be processed to derive integrated intensity of each diffraction spot. (C) 1998 Elsevier Science B.V. All rights reserved., ELSEVIER SCIENCE BV
PHYSICA B, 1997年12月, ［査読有り］

[ (R) -1-シアノエチル-d^α] (ピリジン) コバロキシム錯体の単結晶中性子回折
大原 高志; 植草 秀裕; 大橋 裕二; 田中 伊知朗; 熊澤 紳太郎; 新村 信雄, The Crystallographic Society of Japan
日本結晶学会誌, 1997年

Diffractometer for neutron crystallography in biology
N. Niimura; I. Tanaka; Y. Minezaki; Y. Karasawa; I. Tanaka; K. Miki; M. Sato; M. Hidaka; N. Minekawa; Y. Morii
Physica B, 1995年, ［査読有り］

「研究室便り」―茨城大学でのJ-PARC建設プロジェクトと関連教育・研究―
田中伊知朗
茨城大学工学部同窓会「会報」, 2019年04月, ［招待有り］

副作用の少ない骨粗しょう症薬剤の開発につながる新たな知見,（ 茨城県中性子ビームライン）
横山武司、田中伊知朗、日下勝弘
J-PARC NEWS, 2016年04月28日, ［査読有り］, ［招待有り］

副作用の少ない骨粗しょう症薬剤の開発につながる新たな知見,（ 茨城県中性子ビームライン）
横山武司、田中伊知朗、日下勝弘
J-PARC NEWS HP版, 2016年04月28日, ［査読有り］, ［招待有り］

X-Ray Structure Analyses and Preliminary ESR Experiments of Lysozyme Crystal Induced by TEMPOL towards Neutron Protein Crystallography with Nuclear Polarization Technique (Japanese)
KOMATSUZAKI Naoya; TANAKA Ichiro
Photon Factory Activity Report 2014 #32(2015) B, 2015年

X-Ray Structure Analyses of the Complexes of Kinase Protein DAPK and 2 Kinds of ATP-Analog (Japanese)
MATSUO Yuhei; TANAKA Ichiro
Photon Factory Activity Report 2014 #32(2015) B, 2015年

平成25年度卒業・修了予定者就職情報 生体分子機能工学科
茨城大学工学部後援会会報平成26年3月, 2014年02月

中性子回折計の標準タンパク質結晶探索に向けた単斜晶リゾチームのX線解析沈殿剤としたリゾチームタンパク質のヨウ素配位
小林政義; 田中伊知朗
Photon Factory Activity Report 2013 #31(2014) B, 2014年

入門講座「中性子生物」（8）生体分子の中性子単結晶回折（第二回）タンパク質中性子結晶構造解析のための試料作成、回折計、測定およびデータ処理
田中伊知朗、日下勝弘
日本中性子科学会誌｢波紋｣, 2013年11月, ［査読有り］

JRR‐3BIX‐3およびJ‐PARC iBIX広角中性子回折測定システムを利用した高分子結晶構造解析の展開:極限結晶物性精密評価に必要な基礎的情報収集を目指して
田代孝二; 山元博子; 塙坂真; 日下勝弘; 細谷孝明; 田中伊知朗; 大原高志; 新村信雄
高分子学会予稿集(CD-ROM), 2013年08月28日

JPARC iBIXシステムにおける飛行時間型広角中性子回折測定に基づく合成高分子結晶構造解析の試み
田代孝二; 山元博子; 日下勝弘; 細谷孝明; 田中伊知朗; 大原高志
高分子学会予稿集(CD-ROM), 2013年05月14日

トランスサイレチンにおける水素ネットワークとpH感受性
横山武司,水口峰之、日下勝弘; 田中伊知朗; 新村信雄
日本中性子科学会誌｢波紋｣, 2013年05月, ［査読有り］

Death-associated protein kinase and ATP analogues complex crystallization phase diagram for neutron crystallography
Atsushi Yamaguchi; Nobuo Niimura; Taro Yamada; Ichiro Tanaka
Photon Factory Activity Report 2012 #30 B, 2013年

「Ｊ－ＰＡＲＣの復活」 －中性子科学の現状 －
田中伊知朗
ATI news, 2012年06月

iBIXを利用したアミロイド性タンパク質の中性子結晶構造解析
横山武司,水口峰之、田中伊知朗; 新村信雄
中性子産業利用推進協議会 季報「四季」Vol.15（2012）6-7, 2012年06月

X-ray/neutron joint refinements of Serine Proteases
Taro YAMADA; Kenji KAWAMURA; Yuki OHNISHI; Takeshi YOKOYAMA; Ichiro TANAKA; Kazuo KURIHARA; Taro TAMADA; Ryota KUROKI; Nobuo NIIMURA
Photon Factory Activity Report 2010 #28 Part B, 2012年

Time of Flight Neutron Crystallographic analysis of Human Carbonmonoxyhemoglobin
T. Chatake; N. Shibayama; S.Y. Park; K. Tomoyori; T. Hosoya; T. Ohhara; K. Kusaka; K. Kurihara; I. Tanaka; N. Niimura; Y. Morimoto
1st Asia-Oceania Conference on Neutron Scattering AONSA 2011, 2011年11月01日, ［査読有り］

22aJA-3 臭化鉛一次元結晶の結晶構造と相転移(22aJA X線・粒子線(中性子),領域10(誘電体,格子欠陥,X線・粒子線,フォノン))
高橋 美和子; 高野 幸太; 川崎 卓郎; 大原 高志; 日下 勝弘; 田中 伊知郎; 細谷 孝明; 山田 太郎; 栗原 和男; 新村 信雄
日本物理学会講演概要集, 2011年08月24日

臭化鉛一次元結晶の結晶構造と相転移
高橋美和子; 高野幸太; 川崎卓郎; 大原高志; 日下勝弘; 田中伊知郎; 細谷孝明; 山田太郎; 栗原和男; 新村信雄
日本物理学会講演概要集, 2011年08月24日

Preliminary neutron crystallographic study of mutant Transthyretin
Takeshi Yokoyama; Yuko Nabeshima; Takaaki Hosoya; Takashi Ohhara; Kazuo Kurihara; Katsuhiro Kusaka; Mineyuki Mizuguchi; Ichiro Tanaka; Nobuo Niimura
Acta Cryst. A, 2011年08月

Developments for Upgrades of 2-Dimension Scintillator Detector System, Data Acquisition Electronics and Software for J-PARC
Takaaki Hosoya,a; Tatsuya Nakamura; c; Masaki Katagiri; Masumi Ebine; Atsuhi Birumachi; Katsuhiro Kusaka; Katsuaki Tomoyori; Taro Yamada; Takeshi Yokoyama; Takashi Ohhara,c,e Kazuo; Kurihara,c Nobuo Niimura; Ichiro Tanaka,a; Kazuhiko Soyama
Acta Cryst. A, 2011年08月

Crystal structure of C4H8ONH2-PbBr3 by neutron and X-ray diffraction experiments
Takuro Kawasaki; Kota Takano; Miwako Takahashi; b Takashi; Ohhara,a,c Ken-ichi Ohshima; Katsuhiro Kusaka; Ichiro Tanaka; Taro Yamada; Takaaki Hosoya; Kazuo Kurihara; Nobuo Niimura
Acta Cryst. A, 2011年08月

Proton polarization technique for neutron protein crystallography (NPC)
N.Niimura; T.Chatake; I.Tanaka; K.Kusaka
Acta Cryst. A, 2011年08月

Overview of the IBARAKI biological crystal diffractometer (iBIX) at J-PARC
Ichiro Tanaka,a; Katsuhiro Kusaka; Takaaki Hosoya,a; Kurihara Kazuo; c; Takashi Ohhara,c; Taro Yamada; Katsuaki Tomoyori; Takeshi Yokoyama; Nobuo Niimura
Acta Cryst. A, 2011年08月

The first neutron structure analysis of protein with ibix in j-parc
Katsuhiro Kusaka; Taro Yamada; Takaaki Hosoya,a Takashi; Ohhara,b,c; Kazuo Kurihara; Katsuaki Tomoyori; Takeshi Yokoyama; Ichiro Tanaka; Nobuo Niimura
Acta Cryst. A, 2011年08月

中性子回折を利用したヒトα‐トロンビン‐ビバリルジン複合体の結晶構造解析
山田太郎; 栗原和男; 玉田太郎; 川村健治; 田中伊知朗; 黒木良太; 新村信雄
日本薬学会年会要旨集, 2011年03月05日

擬単結晶(MOMA)を用いた中性子単結晶構造解析の可能性
木村史子; 日下勝弘; 松本弘子; 大原高志; 大原高志; 田中伊知朗; 友寄克亮; 横山武司; 木村恒久
日本磁気科学会年会プログラム・要旨集, 2011年

セリンプロテアーゼの中性子単結晶構造解析
山田太郎; 大西裕季; 川村健治; 栗原和男; 玉田太郎; 田中伊知朗; 正木武治; 黒木良太; 新村信雄
日本結晶学会年会講演要旨集, 2011年

2次元広角中性子回折法に基づく高分子結晶構造解析
田代孝二; 塙坂真; 大原高志; 栗原和男; 黒木良太; 玉田太郎; 藤原悟; 田中伊知朗; 新村信雄
繊維学会予稿集, 2010年06月16日

J-PARC茨城県生命物質構造解析装置(iBIX)による初のタンパク質中性子構造解析
日下勝弘; 山田太郎; 細谷孝明; 友寄克亮; 横山武司; 大西裕季; 田中伊知朗; 新村信雄; 大原高志; 栗原和男
日本結晶学会年会講演要旨集, 2010年

トリプシン‐BPTI複合体の触媒3残基のプロトン化状態と接触領域のH/D交換の観測
川村健治; 山田太郎; 田中伊知朗; 新村信雄; 栗原和男; 玉田太郎; 黒木良太
日本中性子科学会年会講演概要集, 2010年

ヒト‐トロンビン阻害剤複合体における水和構造
山田太郎; 川村健治; 大西裕季; 田中伊知朗; 新村信雄; 栗原和男; 玉田太郎; 黒木良太
日本中性子科学会年会講演概要集, 2010年

中性子構造生物学の現在と未来
田中伊知朗
日本結晶学会誌, 2009年02月, ［査読有り］, ［招待有り］

トリプシン‐BPTI複合体結晶のX線・中性子結晶構造解析
川村健治; 山田太郎; 田中伊知朗; 新村信雄; 高橋東之; 栗原和男; 玉田太郎; 黒木良太
日本中性子科学会年会講演概要集, 2009年

T6ブタインスリンの中性子結晶構造解析
岩井和加里; 山田太郎; 大西裕季; 小林陽一郎; 田中伊知朗; 高橋東之; 新村信雄; 栗原和男; 黒木良太; 玉田太郎
日本中性子科学会年会講演概要集, 2009年

トロンビン‐ビバリルジン複合体のX線・中性子結晶構造解析
山田太郎; 大西裕季; 田中伊知朗; 新村信雄; 栗原和男; 玉田太郎; 黒木良太
日本中性子科学会年会講演概要集, 2009年

IUCr2008サテライト会議「Symposium on Neutron Protein Crystallography」
田中伊知朗、玉田太郎
日本中性子科学会誌｢波紋｣, 2008年10月, ［査読有り］

重水素化および軽水素化高分子延伸試料の2次元広角中性子回折データに基づく結晶構造解析
塙坂真; 田代孝二; 大原高志; 栗原和男; 黒木良太; 玉田太郎; 藤原悟; 田中伊知郎; 新村信雄; 北野利明; 二宗隆; 勝部勝義; 森川桂介; 古宮行淳
高分子学会予稿集(CD-ROM), 2008年09月09日

A new biological neutron diffractometer (iBIX) in J-PARC
I. Tanaka; K. Kusaka; K. Tomoyori; N. Niimura; T. Ohhara; K. Kurihara; T. Hosoya; T. Ozeki
Acta Cryst. A, 2008年08月

Optimization of design parameters of IBARAKI Biological Crystal Diffractometer (iBIX) in J-PARC
K. Kusaka; T. Ohhara; K. Kurihara; I. Tanaka; T. Hosoya; K. Tomoyori; T. Ozeki; N. Niimura
Acta Cryst. A, 2008年08月

Optics and shielding of IBARAKI Biological Crystal Diffractometer (iBIX) in J-PARC
K. Kurihara; T. Ohhara; K. Kusaka; K. Nitta; T. Hosoya; K. Tomoyori; N. Niimura; I. Tanaka
Acta Cryst. A, 2008年08月

Development of data processing software for a TOF single crystal neutron diffractometer at J-PARC
T. Ohhara; K. Kusaka; T. Hosoya; K. Kurihara; K. Tomoyori; N. Niimura; I. Tanaka; J. Suzuki; T. Nakatani; T. Otomo; S. Matsuoka; K. Tomita; Y. NishimakiT. Ajima; S. Ryufuku
Acta Cryst. A, 2008年08月

Crystallization of serine proteases for neutron single crystal structure determination
T. Yamada; K. Kawamura; Y. Onishi; T. Ishikawa; K. Kusaka; I. Tanaka; N. Niimura
Acta Cryst. A, 2008年08月

X-ray diffuse scattering from protein crystals causedby the lattice defects
K. Kawamura; N. Niimura; I. Tanaka; Y. Ohnishi; T. Yamada
Acta Cryst. A, 2008年08月

Large single crystal growth and preliminary neutron diffraction analysis of Achromobacter protease I
Y. Ohnishi; T. Masaki; T. Yamada; K. Kurihara; I. Tanaka; N. Niimura
Acta Cryst. A, 2008年08月

Methyl group configuration and hydrogen bonds in proteins determined by neutron crystallography
K. Shibata; A. Yamaguchi; I. Tanaka; N. Niimura
Acta Cryst. A, 2008年08月

The effect of deutererium oxide on hydration structure of proteinase K
T. Ishikawa; T. Chatake; I. Tanaka; Y. Morimoto
Acta Cryst. A, 2008年08月

Neutron crystallography of 2Zn insulin
W. Iwai; T. Yamada; Y. Kobayashi; Y. Ohnishi; I. Tanaka; N. Niimura
Acta Cryst. A, 2008年08月

Dynamics phase transition of water cluster stabilized in molecular nanoporous crystal
M. Tadokoro; T. Ohhara; Y. Ohhata; R. Yonamine; I. Tanaka; K. Kurihara; O. Yamamuro; R. Kuroki
Acta Cryst. A, 2008年08月

Application of neutron imaging plate system to crystal structure analysis of deuterated polymers
M. Hanesaka; K. Tashiro; Y. Yoshizawa; T. Kitano; T. Nishu; T. Ohhara; I. Tanaka; N. Niimura; K. Kurihara; R. Kuroki; T. Yamada; T. Tamada; S. Fujiwara; T. Ozeki
Acta Cryst. A, 2008年08月

二次元広角中性子回折図形に基づく一軸配向重水素化ポリエチレンオキシドの結晶構造解析と水素原子位置の抽出
塙坂真; 田代孝二; 大原高志; 栗原和男; 黒木良太; 玉田太郎; 藤原悟; 田中伊知朗; 新村信雄
高分子学会予稿集(CD-ROM), 2008年05月08日

茨城県日立第一高等学校との高大連携講座
田中伊知朗
茨城大学工学部年報 2007年度版, 2008年04月

二次元広角中性子回折データに基づく重水素化高分子配向試料の結晶構造解析
塙坂真; 田代孝二; 吉澤功徳; 平山亮; 北野利明; 二宗隆; 大原高志; 栗原和男; 黒木良太; 玉田太郎; 藤原悟; 田中伊知朗; 新村信雄
高分子学会予稿集(CD-ROM), 2007年09月04日

高分子巨大単結晶の広角中性子回折図形ならびに広角X線回折図形の解析と水素原子位置の直接検出
田代孝二; 塙坂真; 吉澤功徳; 大原高志; 黒木良太; 田中伊知朗; 新村信雄; 松本章一
高分子学会予稿集(CD-ROM), 2007年05月10日

放射光X線回折および中性子回折測定に基づく重水素化および水素化ポリオキシメチレン固相重合試料の精密結晶構造解析
田代孝二; 塙坂真; 北野利明; 二宗隆; 尾関智二; 大原高志; 栗原和男; 黒木良太; 玉田太郎; 藤原悟; 田中伊知朗; 新村信雄
高分子学会予稿集(CD-ROM), 2007年05月10日

放射光X線回折および中性子回折データに基づく水素原子位置抽出を目的としたイソタクチックポリプロピレンの結晶構造解析
塙坂真; 平山亮; 尾関智二; 大原高志; 栗原和男; 黒木良太; 玉田太郎; 藤原悟; 田中伊知朗; 新村信雄
高分子学会予稿集(CD-ROM), 2007年05月10日

タンパク質結晶品質の評価と制御
新村信雄; 吉崎泉; 栗原和男; 大西裕季; 田中伊知朗; 原田繁春; 小島謙一; 玉田太郎; 岩井和香里; 原田一明
宇宙利用シンポジウム, 2007年03月

高分子結晶構造解析の新しい局面の始まり[3]種々の高分子についての中性子構造解析の試み
田代孝二; 塙坂真; 吉澤功徳; 北野利明; 二宗隆; 勝部勝義; 森川桂介; 古宮行淳; 大原高志; 栗原和男; 黒木良太; 玉田太郎; 藤原悟; 田中伊知朗; 新村信雄
日本結晶学会年会講演要旨集, 2007年

高分子結晶構造解析の新しい局面の始まり[1]X線と中性子の利用による水素原子抽出
田代孝二; 塙坂真; 北野利明; 二宗隆; 尾関智二; 大原高志; 栗原和男; 黒木良太; 玉田太郎; 藤原悟; 田中伊知朗; 新村信雄
日本結晶学会年会講演要旨集, 2007年

Detailed comparison of crystal structure information of polydiacetylene obtained by X-ray and neutron diffraction data
Kohji Tashiro; Makoto Hanesaka; Tomoji Ozeki; Takashi Oohara; Kazuo Kurihara; Ryota Kuroki; Taro Tamada; Satoru Fujiwara; Ichiro Tanaka; Nobuo Niimura
Polymer Preprints, Japan, 2006年12月01日

Structure refinement of polyoxymethylene based on wide-angle X-ray diffraction data by utilizing synchrotron X-ray beam of short wavelength and wide-angle neuron diffraction data
Kohji Tashiro; Makoto Hanesaka; Tomoji Ozeki; Ichiro Tanaka; Takashi Oohara; Nobuo Niimura; Kazuo Kurihara; Ryota Kuroki; Taro Tamada; Satoru Fujiwara
Polymer Preprints, Japan, 2006年12月01日

Structural refinement of polyoxymethylene based on wide angle neutron diffraction data
Kohji Tashiro; Makoto Hanesaka; Erathimmanna Bhoje Gowd; Ichiro Tanaka; Takashi Oohara; Nobuo Niimura; Kazuo Kurihara; Ryota Kuroki; Taro Tamada; Satoru Fujiwara
Polymer Preprints, Japan, 2006年10月18日

Growth of Large Single Crystals of Bovine β-Lactoglobulin A on the Basis of Phase Diagram and Characterization of Crystals
D. Yagi; Y. Ohnishi; I. Tanaka; N. Niimura
Proc. 2nd ISCIU, Ed Ibaraki Univ, 2006年10月

Neutron Diffraction from Cubic Insulin at pD6 and 7
T. Ishikawa; Y. Ohnishi; I. Tanaka; N. Niimura
Proc. 2nd ISCIU, Ed Ibaraki Univ., 2006年10月

Crystallization Phase Diagram of α-amylase by a dialysis method
T. Ichige; Y. Ohnishi; I. Tanaka; N. Niimura
Proc. 2nd ISCIU, Ed Ibaraki Univ., 2006年10月

X線および中性子回折データに基づくポリジアセチレン単結晶構造の詳細比較
田代孝二; 塙坂真; 尾関智二; 大原高志; 栗原和夫; 黒木良太; 玉田太郎; 藤原悟; 田中伊知朗; 新村信雄
高分子学会予稿集(CD-ROM), 2006年09月05日

放射光X線回折および中性子回折データを用いたポリオキシメチレンの精密結晶構造解析
田代孝二; 塙坂真; 尾関智二; 田中伊知朗; 新村信雄; 大原高志; 栗原和男; 黒木良太; 玉田太郎; 藤原悟
高分子学会予稿集(CD-ROM), 2006年09月05日

中性子回折によるポリオキシメチレン(POM)の構造精密化
田代孝二; 塙坂真; GOWD Erathimmanna Bhoje; 田中伊知朗; 新村信雄; 大原高志; 栗原和男; 黒木良太; 玉田太郎; 藤原悟
高分子学会予稿集(CD-ROM), 2006年05月10日

中性子産業応用事例集
浅野肇ほか18名(50音順で第9著者)
茨城県企画部企画課, 2006年01月31日

Z-DNA6量体の中性子結晶解析
茶竹俊行; 田中伊知朗; 海野久雄; 新井栄揮; 新村信雄
日本中性子科学会年会講演概要集, 2006年

Recent results on hydrogen and hydration in biology studied by neutron macromolecular crystallography (Invited Review Articles.)
Nobuo Niimura; Shigeki Arai; Kazuo Kurihara; Toshiyuki Chatake; Ichiro Tanaka; Robert Bau
Cell. Mol. Life Sci., 2006年

放射光高エネルギーX線および中性子線を用いた重水素化ならびに軽水素化ポリオキシメレンの全回転回折図形の測定と結晶構造解析
田代孝二; 塙坂真; 二宗隆; 北野利明; 尾関智二; 大原高志; 栗原和男; 黒木良太; 玉田太郎; 藤原悟; 田中伊知朗; 新村信雄
日本中性子科学会年会講演概要集, 2006年

異なる水素イオン濃度における立方晶インスリンの中性子構造解析
石川卓哉; 田中伊知朗; 茶竹俊行; 栗原和男; 大西裕季; 日下勝弘; 玉田太郎; 黒木良太; 新村信雄
日本中性子科学会年会講演概要集, 2006年

放射光高エネルギーX線および中性子線を用いた重水素化ならびに軽水素化ポリオキシメチレンの全回転回折図形の測定と結晶構造解析
田代孝二; 塙坂真; 二宗隆; 北野利明; 尾関智二; 大原高志; 栗原和男; 黒木良太; 玉田太郎; 藤原悟; 田中伊知朗; 新村信雄
日本中性子科学会年会講演概要集, 2006年

Hydrogen and Hydration in Proteins and Nucleic Acids.,Neutron Diffraction from Bio-macromolecules at JAERI
Nobuo Niimura; Shigeki Arai; Kazuo Kurihara; Toshiyuki Chatake; Ichiro Tanaka; Robert Bau
Hydrogen- and Hydration-Sensitive Structural Biology, 2005年07月, ［招待有り］

Direct Observation of the Hydrogen Transfer in the Solid-State Organic Photoreaction by Neutron Diffraction Method
Takaaki Hosoya; H. Uekusa; Y. Ohashi; T. Ohhara; I. Tanaka; N. Niimura
JAERI-Review, Progress Report on Neutron Scattering Research, 2005年

The hydration structure of a Z-DNA hexameric duplex determined by a neutron diffraction tecqunique.
Toshiyuki Chatake; Ichiro Tanaka; Hisao Umino; Shigeki Arai; Nobuo Niimura
Acta Crysta, 2005年

Neutron Diffraction Experiment of DsrD protein
T. Chatake; N. Mizuno; G. Voordouw; Y. Higuchi; I. Tanaka; N. Niimura
JAERI-Review, 2004年

Neutron Diffraction Experiment of Cubic Insulin Crystal
Neutron Diffraction Experiment of Cubic Insulin Crystal
JAERI-Review, 2004年

3P035 ヒトリゾチームの中性子結晶構造解析により観測された局在水素及び水和水による部位特異的ペプチド結合の歪み(蛋白質 C) 物性 : 安定性、折れたたみなど)
千葉 かおり; 松井 拓郎; 茶竹 俊行; 大原 高志; Ostermann Andreas; 田中 伊知朗; 油谷 克英; 新村 信雄
生物物理, 2004年

”Complicated Water Network in the Minor Groove of B-DNA Decamer\nd(CCATTAATGG)2 observed by Neutron Diffraction Measurements”
S. Arai; T. Chatake; T. Ohhara; K. Kurihara; I. Tanaka; N. Suzuki; Z. Fujimoto; H. Mizuno; N. Niimura
The 5th International Conference on Biological Physics\n, 2004年

2P006 ヒトヘモグロビンの中性子回折による構造研究(蛋白質 A) 構造)
森本 幸生; 朴 三用; 柴山 修哉; 栗原 和男; 田中 伊知朗; 玉田 太郎; 黒木 良太; 新村 信雄
生物物理, 2004年

Deuterium Migration Mechanism in Chiral Thiolactam Formation by Neutron Diffraction Analysis
Takaaki Hosoya; T. Hosoya; H. Uekusa; Y. Ohashi; T. Ohhara; I. Tanaka; N. Niimura
JAERI-Review, Progress Report on Neutron Scattering Research, 2004年

生体高分子用中性子回折装置BIX‐3,BIX‐4による最近の研究成果(2004年)
栗原和男; 玉田太郎; 大原高志; 田中伊知朗; 新村信雄; 黒木良太
日本中性子科学会年会講演概要集, 2004年

ヒトヘモグロビンの中性子回折による構造研究
森本幸生; PARK S. Y; 柴山修哉; 栗原和男; 田中伊知朗; 玉田太郎; 黒木良太; 新村信雄
日本中性子科学会年会講演概要集, 2004年

世界最高性能を誇る中性子回折装置
新村信雄、栗原和男、田中伊知朗
化学同人「化学」, 2004年, ［招待有り］

B型DNA+量体d(CCATTAATGG)の中性子結晶構造解析
新井 栄揮; 茶竹 俊行; 栗原 和男; 田中 伊知朗; 大原 高志; 新村 信雄
生物物理, 2003年

DsrD蛋白質の中性子結晶構造解析
茶竹 俊行; 水野 伸宏; 樋口 芳樹; Voordouw Gerrit; 田中 伊知郎; 新村 信雄
生物物理, 2003年

インスリンの中性子構造解析
前田 満; 茶竹 俊行; 田中 伊知朗; 栗原 和男; 新村 信雄
生物物理, 2003年

Neutron Crystallography of Human Lysozyme
Neutron Crystallography of; Human Lysozyme
JAERI-Review, 2002年

中性子回折計BIX-3が拓く新しい構造の世界
新村信雄; 田中伊知朗; 栗原和男; 茶竹俊行; A.Ostermann; 大原高志
波紋, 2002年

A high-performance neutron diffractometer for biological crystallography (BIX-3)
I.Tanaka; K.Kurihara; T.Chatake; N.Niimura
J. appl. Cryst., 2002年

A neutron crystallographic analysis of a rubredoxin mutant
T.Chatake; K.Kurihara; I.Tanaka; M.W.W.Adams; F.E.Jenney Jr; I.Tsyba; R.Bau; N.Niimura
Applied Physics, 2002年

Hydrogen and Deuterium in Myoglobin as seen by a Neutron Structure Determination at 1.5Å Resolutio
A.Ostermann; I. Tanaka; N.Engler; N.Niimura; F.G. Parak
Biophysical Chem., 2002年

中性子回折計BIX-3によるこの1年の成果
田中伊知朗; 栗原和男; 茶竹俊行; 新井栄樹; OSTERMANN A; 大原高志; 千葉薫; 新村信雄
日本中性子科学会年会講演概要集, 2001年

2P244チトクロームc'の結晶成長機構に関する研究
渡邊 博義; 高妻 孝光; 中村 裕彦; 依田 真一; 山中 亜利; Ostermann Andreas; 栗原 和男; 茶竹 俊行; 田中 伊知郎; 新村 信雄
生物物理, 2001年

A new single crystal diffractometer for neutron protein crystallography (BIX-3M)
K.Kurihara; I.Tanaka; T.Chatake; A.Ostermann; N.Niimura
The International Conference on Neutron Scattering 2001\n, 2001年

原研中性子構造生物学の現状
新村信雄; 田中伊知朗; 栗原和男; 茶竹俊行; A.Ostermann
構造生物, 2001年

Neutron Diffractometer for Biological Crystallography (BIX-3)
I.Tanaka; K.Kurihara; T.Chatake; N.Niimura
J. Phys. Soc. Jpn., 2001年

Neutron Diffraction Study on the Structure of Rubredoxin from Pyrococcus furiosus
K.Kurihara; I.Tanaka; M.W.W.Adams; F.E.Jenney Jr; N.Moiseeva; R.Bau; N.Niimura
J. Phys. Soc. Jpn., 2001年

Single Crystal Neutron Diffraction Study of the 3-2-1 Two step Photoisomerization of 3-Cyanopropyl Cobaloxim Complex
T.Ohhara; H.Uekusa; Y.Ohashi; I.Tanaka; N.Niimura
J.Phys.Soc.Jpn., 2001年

Analysis of Crystalline-State Photo-Racemization of a Cobaloxime Complex Containing Bulky Substituents
Hiroyuki Imura; Takashi Ohhara; Hidehiro Uekusa; Tomoji Ozeki; Yuji Ohashi; Ichiro Tanaka; Kazuo Kurihara; Nobuo Niimura
J. Phys. Soc. Jpn., 2001年

Small-angle Neutron Scattering Study on a Proteoglycan in Solution
Yasushi Watanabe; Ichiro Tanaka; Yoh Sano; Nobuo Niimura
J. Phys. Soc., 2001年

Direct observation of deuterium migration in crystalline-state reaction by single-crystal neutron diffraction. III. Photoracemization of 1-cyanoethyl cobaloxime complexes
Takashi Ohhara; Hidehiro Uekusa; Yuji Ohashi; Ichiro Tanaka; Nobuo Niimura
Acta Cryst., 2001年

新型生体物質中性子回折装置の開発とそれによるタンパク質の水素位置決定
田中伊知朗; 栗原和男; 新村信雄
Isotope News 2000, 2000年

Direct observation of deuterium migration in crystalline – state reaction by single crystal neutron diffraction. II. 3-1 Photpisomerization of a cobaloxim complex.
T. Ohhara; J. Harada; Y. Ohashi; I. Tanaka; S. Kumazawa; N.Niimura
Acta Cryst., 2000年

Performance of a multi-wavelength monochromator system for neutron single crystal and powder diffraction
F.U.Ahmed; I.Tanaka; N.Niimura
J.Appl.Cryst., 2000年

Polar Structure of Lysozyme Aggregates in Unsaturated Solution Determined by Small Angle Neutron Scattering Contrast Variation Method
N.Niimura; Y.Minezaki; I.Tanaka; S.Fujiwara; M.Ataka
J. Crystal Growth, 1999年

The Classical Structure of TaCp2(H)(SiMe2H)2
Ichiro Tanaka; Takashi Ohhara; Nobuo Niimura; Yuji Ohashi; Qian Jiang; Donald H. Berry; Robert Bau
J. Chem. Research (S), 1999年

An elastically bent silicon monochromator for a neutron diffractometer
Ichiro Tanaka; Nobuo Niimura; Pavel Mikula
J. Appl. Cryst, 1999年

An upgradede neutron diffractometer (BIX-IM) for macromolecules with a neutron imaging plate
I.Tanaka; K.Kurihara; Y.Haga; Y.Minezaki; S.Fujiwara; S.Kumazawa; N.Niimura
J. Phys. Chem. Solids., 1999年

Mechanism of deuterium - hydrogen exchange in the photoisomerization of cobalt complex
Y.Ohashi; T.Ohhara; J.Harada; I.Tanaka; S.Kumazawa; N.Niimura
J. Phys. Chem. Solids., 1999年

Data Acquisition of Neutron Crystallography on Tetragonal and Triclinic Form of Hen Egg-White (HEW) Lysozyme with an Elastically Bent Si Monochromator.
I.Tanaka; M.Minezaki; K.Harada; N.Niimura
Physica, 1998年

Direct Observation of Correlation between Crystalline-State Deuterium Transfer and Racemization of 1-Cyanoethylcobaloxime Complex by Neutron diffraction
T.Ohhara; H.Uekusa; Y.Ohashi; I.Tanaka; S.Kumazawa; N.Niimura
Chem. Letters, 1998年

CROSSOVER OF LYSOZYME AGGREGATES BETWEEN SUPER- AND UNDER- SATURATED STATES IN AQUEOUS SOLUTION.
N. Niimura; M. Ataka; I. Tanaka; Y. Minezaki; Y. Karasawa
ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, 1996年

A Monochromator for Neutron Crystallography in Biology
N.Niimura; I.Tanaka; Y.Karasawa; N.Minakawa
Physica, 1995年

The Structure of Gelsolin-PIP2 Complex as Studied by Small Angle Neutron Scattering
T.Ito; J.Fukushima; Y.Minezaki; I.Tanaka; N.Niimura; K.Hayashi
JAERI-M, 1993年

Small Angle Neutron Scattering Studies of Proteoglycan from Shark Fin Cartilage
Y.Sano; N.Niimura; I.Tanaka
JAERI-M;, 1993年

Small Angle Neutron Scattering Study of the Initial Stage of Lysozyme Crystallization Process
Y.Minezaki; I.Tanaka; N.Niimura; M.Ataka; T. Katsura
JAERI-M, 1993年

Small-Angle Neutron Scattering Studies of Proteoglycan from Shark FIN Cartilage in 100% and 0% D2O/H2O Solution
Y.Sano; N.Niimura; I.Tanaka
KENS REPORT 9, 1993年

Small Angle Neutron Scattering Study of the Initial Stage of Lysozyme Crystallization Process
Y.Minezaki; I.Tanaka; N.Niimura; M.Ataka; T.Katsura
Proc. Inter. Sympo. Adv. Nucl. Energy Res . JAERI-M 93-228, 1993年

Solution Scattering Study of Bacterial Histone-like Protein HU and DNA Complex
I.Tanaka; N.Niimura; T.Miyaji; I.Tanaka; M.Kataoka; R.K.Heenan
8-th Yokohama Forum for the 21st Century International Symposium on Molecular Structure and Life-Molecular Recognition of Nucleic Acids-, 1991年

Current status and near future plan of neutron protein crystallography at J-PARC(in press)　　　　　　　　　　　　　　　
Ichiro TANAKA; Toshiyuki CHATAKE; Satoru FUJIWARA; Takaaki HOSOYA; Katsuhiro KUSAKA; Nobuo NIIMURA; Taro YAMADA; Naomine YANO, 共著
Neutron Crystallography in Structural Biology, Methods in enzymology, vol.634, Ed. Peter Moody, 2020年

Protonation/Deprotonation of Proteins by Neutron Diffraction Structure Analysis in "The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery" (Ed. Makoto Suzuki)
Ichiro Tanaka; Katsuhiro Kusaka; Nobuo Niimura, 共著
Springer Nature Singapore Pte Ltd., 2018年05月11日
9789811084584

Application of Neutron Diffraction in Studies of Protein Dynamics and Functions　　　　　　　　　　　　　　　
N. Niimura; M. Takimoto-Kamimura; I. Tanaka, 共著
Encyclopedia of Analytical Chemistry, JohnWiley & Sons, Ltd., 2016年06月27日

放射線を学ぼう！！！　　　　　　　　　　　　　　　
菊地賢司、新村信雄、関東康祐、田中伸厚、車田亮、田中伊知朗、高橋東之, 共著
茨城大学特定課題震災対応-放射線教育と日立地区線量率計測班パンフレット作成グループ-, 2011年11月

パルス中性子回折散乱実験入門　　　　　　　　　　　　　　　
共編者(共編著者)
企画・編集 田中伊知朗、新村信雄, 2009年03月

Hydrogen- and Hydration-Sensitive Structural Biology　　　　　　　　　　　　　　　
N. Niimura; S. Arai; K. Kurihara; T. Chatake; I. Tanaka; R. Bau, 共著
Kuba Pro Co. Ltd., Tokyo, Japan, 2005年07月
4878050616

タンパク質多結晶の核偏極中性子回折実験　　　　　　　　　　　　　　　
田中伊知朗; 山内秀輝; 能田洋平; 前田知貴; 小泉智
2022年度量子ビームサイエンスフェスタ, 2023年03月15日
20230313, 20230315

微小流路デバイスによる大形結晶育成法のさまざまなタンパク質への適用　　　　　　　　　　　　　　　
齋藤 洋也、小泉 怜、新村 信雄、田中 伊知朗
2022年度量子ビームサイエンスフェスタ, 2023年03月15日
20230313, 20230315

セリンプロテアーゼ加水分解反応後半部分の中性子解析に向けた結晶化　　　　　　　　　　　　　　　
武田 和久、田中 伊知朗
2022年度量子ビームサイエンスフェスタ, 2023年03月15日
20230313, 20230315

微小流路デバイスを用いたタンパク質大形結晶育成の試み　　　　　　　　　　　　　　　
小泉 怜、齋藤 洋也、新村 信雄、田中 伊知朗
2022年度量子ビームサイエンスフェスタ, 2023年03月15日
20230313, 20230315

核偏極中性子回折実験における高偏極化を目指した脱酸素条件でのタンパク質単結晶化の考察　　　　　　　　　　　　　　　
大石 翼、能田 洋平、前田 知貴、小泉 智、田中 伊知朗
2022年度量子ビームサイエンスフェスタ, 2023年03月15日
20230313, 20230315

汚染土壌における経済的除染方法開発のための放射性Cs溶出条件の探索　　　　　　　　　　　　　　　
杉原 誠、菊地 賢司、新村 信雄、田中 伊知朗
2022年度量子ビームサイエンスフェスタ, 2023年03月15日
20230313, 20230315

水素情報を含めたリゾチームの糖加水分解機構解明のための構造学的研究　　　　　　　　　　　　　　　
鴨崎 真仁、田中 伊知朗
2022年度量子ビームサイエンスフェスタ, 2023年03月15日
20230313, 20230315

微小流路を用いた大形良質タンパク質結晶育成法　　　　　　　　　　　　　　　
田中伊知朗,齋藤洋也,小泉怜
⽇本結晶学会2022年度年会, 2022年11月27日
20221126, 20221127

リゾチーム -NAG 複合体の中性子解析による反応機構解明に向けて　　　　　　　　　　　　　　　
鴨崎 真仁、田中 伊知朗
日本中性子科学会 第22回年会, 2022年10月27日
20221026, 20221028

D/Hコントラスト法を中心とした蛋白質の水和構造解析の現状　　　　　　　　　　　　　　　
茶竹 俊行,田中 伊知朗,日下 勝弘,角南 智子,藤原 悟
日本中性子科学会 第22回年会, 2022年10月27日
20221026, 20221028

Neutron crystallography of hen-egg white lysozyme using D/H contrast technique　　　　　　　　　　　　　　　
Toshiyuki Chatake; Ichiro Tanaka; Katsuhiro Kusaka; Satoru Fujiwara
第60回日本生物物理学会年会, 2022年09月30日
20220928, 20220930

Technological development for high-sensitivity detection of hydrogen in protein neutron diffraction experiments　　　　　　　　　　　　　　　
Ichiro Tanaka; Hideki Yamauchi; Yohei Noda; Tomoki Maeda; Satoshi Koizumi
第60回日本生物物理学会年会, 2022年09月30日
20220928, 20220930

Reconsideration of hydrolysis reaction mechanism by lysozyme-NAG complex crystal structure analysis　　　　　　　　　　　　　　　
Ichiro Tanaka; Masahito Kamosaki
Molecular Movies International Symposium 2022, 2022年05月13日
20220512, 20220513

マイクロ流路を用いた大形良質タンパク質結晶育成法の確立　　　　　　　　　　　　　　　
長谷川智紀; 根岸政也; 齋藤洋也; 田中伊知朗; 新村信雄; 山田貢; 石田卓也; 吉崎泉; 皆川由貴; 伊藤剛士; 蛭田佳樹; 真栄城正寿
2021年度量子ビームサイエンスフェスタ, 2022年03月09日
20220307, 20220309

タンパク質の動的核偏極中性子回折実験　　　　　　　　　　　　　　　
田中伊知朗; 能田洋平; 前田智貴; 小泉智
2021年度量子ビームサイエンスフェスタ, 2022年03月09日
20220307, 20220309

リゾチーム-NAG 複合体の中性子解析による反応機構考察　　　　　　　　　　　　　　　
鴨崎真仁; 茶竹俊行; 山田太郎; 矢野直峰; 日下勝弘; 田中伊知朗
2021年度量子ビームサイエンスフェスタ, 2022年03月09日
20220307, 20220309

リゾチーム反応機構解明に向けた反応遅延条件での結晶化の試み　　　　　　　　　　　　　　　
小池佑季; 大林美咲; 鴨崎真仁; 田中伊知朗
2021年度量子ビームサイエンスフェスタ, 2022年03月09日
20220307, 20220309

マイクロ流路による大形良質結晶育成法のグルコースイソメラーゼへの適用　　　　　　　　　　　　　　　
齋藤洋也; 長谷川智紀; 田中伊知朗; 新村信雄; 山田貢; 石田卓也; 吉崎泉; 皆川由貴; 伊藤剛士; 蛭田佳樹; 真栄城正寿
2021年度量子ビームサイエンスフェスタ, 2022年03月08日
20220307, 20220309

マイクロ流路による大形良質タンパク質結晶育成法の精密化とソーマチンへの適用　　　　　　　　　　　　　　　
根岸 政也; 齋藤 洋也; 長谷川 智紀; 田中 伊知朗
2021年度量子ビームサイエンスフェスタ, 2022年03月08日
20220307, 20220309

ミュオンによるセリンプロテアーゼ加水分解反応観測　　　　　　　　　　　　　　　
小柳文哉; 田中伊知朗; 清谷多美子; 新村信雄; 中村惇平; 西村昇一郎; 幸田章宏; 平石雅俊
2021年度量子ビームサイエンスフェスタ, 2022年03月08日
20220307, 20220309

リゾチーム 反応機構解明に向けた糖鎖の結合様式の研究　　　　　　　　　　　　　　　
大林美咲; 小池祐季; 鴨崎真仁; 田中 伊知朗
2021年度量子ビームサイエンスフェスタ, 2022年03月08日
20220307, 20220309

〔主要な業績〕Reaction mechanism study of lysozyme-NAG complex by neutron crystallography　　　　　　　　　　　　　　　
Masahito Kamozaki; Ichiro Tanaka
The 6th International Symposium of Quantum Beam Science at Ibaraki University, 2022年02月22日, Ibaraki University
20220221, 20220222

〔主要な業績〕Protein neutron diffraction experiment with dynamic nuclear polarization　　　　　　　　　　　　　　　
Ichiro Tanaka; Himeka Nishino; Hideki Yamauchi; Yohei Noda; Tomoki Maeda; Satoshi Koizumi
The 6th International Symposium of Quantum Beam Science at Ibaraki University, 2022年02月21日, Ibaraki University, ［招待有り］
20220221, 20220222

〔主要な業績〕Analysis of serine protease hydrolysis by muon　　　　　　　　　　　　　　　
Fumiya Koyanagi; Ichiro Tanaka
The 6th International Symposium of Quantum Beam Science at Ibaraki University, 2022年02月21日, Ibaraki University, ［招待有り］
20220221, 20220222

Analysis of internal magnetic field induced from electron and proton transfer during serine protease hydrolysis by µSR　　　　　　　　　　　　　　　
Fumiya Koyanagi; Ichiro Tanaka; Tamiko Kiyotani; Nobuo Niimura; Jumpei Nakamura; Shoichiro Nishimura; Akihiro Koda
Materials Research Meeting 2021, 2021年12月16日
20211213, 20211217

〔主要な業績〕Detection of Functional Processes of Photoreceptive Proteins by Muon　　　　　　　　　　　　　　　
Keiichi Inoue; Tamiko Kiyotani and Ichiro Tanaka
ISIS Muons Illumination Workshop, 2021年12月16日, ISIS (UK), ［招待有り］
20211216, 20211216

〔主要な業績〕動的核偏極技術を用いたタンパク質の中性子回折実験　　　　　　　　　　　　　　　
田中伊知朗; 山内秀輝; 能田洋平; 前田知貴; 小泉智
日本中性子科学会年会 2021, 2021年12月03日, 日本中性子科学会
20211201, 20211203

〔主要な業績〕リゾチーム-NAG複合体の中性子結晶構造解析　　　　　　　　　　　　　　　
田中伊知朗; 西野宮良太; 鴨崎真仁; 茶竹俊行; 日下勝弘; 矢野直峰; 山田太郎
日本結晶学会2021年度年会, 2021年11月19日, 日本結晶学会
20211119, 20211121

〔主要な業績〕加水分解機構全容解明に向けたX線・中性子による糖リゾチーム複合体解析　　　　　　　　　　　　　　　
田中伊知朗
令和３年度 新学術領域研究「高速分子動画」領域会議, 2021年11月01日, 新学術領域研究「高速分子動画」
20211101, 20211102

〔主要な業績〕タンパク質の生成結晶核数の制御を可能とする微小流路デバイス　　　　　　　　　　　　　　　
田中伊知朗
JST新技術発表会, 2021年09月14日, JST
20210914, 20210914

〔主要な業績〕Protein neutron diffraction experiment with dynamic nuclear polarization　　　　　　　　　　　　　　　
Ichiro Tanaka; Himeka Nishino; Hideki Yamauchi; Yohei Noda; Tomoki Maeda; Satoshi Koizumi
25th congress of the International Union of Crystallography(IUCr2021), 2021年08月19日, IUCr(Czech), ［招待有り］
20210814, 20210822

高速酵素反応機構解明のための糖リゾチーム複合体構造解析と加水分解速度の制御　　　　　　　　　　　　　　　
田中伊知朗
第9回高速分子動画オンラインセミナー(zoom), 2021年06月01日, 新学術領域研究「高速分子動画」, ［招待有り］
20210601, 20210601

高速酵素反応機構解明のための糖リゾチーム複合体構造解析と加水分解速度の制御　　　　　　　　　　　　　　　
田中伊知朗; 鴨崎真仁; 梅田翔希; 西ノ宮良太; 茶竹俊行
令和３年度 新学術領域研究「高速分子動画」領域会議, 2021年05月17日, 新学術領域研究「高速分子動画」
20210517, 20210517

〔主要な業績〕Dissolution, Mechanical Properties, and Thermal Stability of Microparticles Containing Radioactive Cesium on Plant Litter Derived from the Fukushima Daiichi Nuclear Power Plant Accident, and Soil Decontamination Trials　　　　　　　　　　　　　　　
Ichiro Tanaka; Atsushi Yamaguchi; Kenji Kikuchi; Nobuo Niimura; Yume Saeki; Makoto Sugihara
European Geosciences Union General Assembly 2021(vEGU21), 2021年04月26日, ［招待有り］
20210419, 20210430

Second target station as an upgraded neutron pulsed source in Japan will open the new era of neutron protein crystallography　　　　　　　　　　　　　　　
Ichiro Tanaka
AsCA2019, 2019年12月
20191216, 20191220

Direct Observation of Electron and Proton Transfers in Enzymatic Reactions by μSR　　　　　　　　　　　　　　　
Tamiko Kiyotani; Ichiro Tanaka; Nobuo Niimura
Materials Research Meeting 2019, 2019年12月11日
20191210, 20191214

Recent Structural Study Insight into Lysozyme Hydrolysis Mechanism　　　　　　　　　　　　　　　
Tanaka, Ichiro; Nishinomiya, Ryota
The 6th International Symposium on Diffraction Structural Biology (ISDSB2019), 2019年10月18日, Japan Society for the Promotion of Science, University-Industry Research Cooperative Research Committee, 169th Committee on Structural Biology using Diffraction
20191017, 20191020

高感度水素検出による生体内化学反応の制御を目指して,はじめに　　　　　　　　　　　　　　　
田中 伊知朗、石北 央
日本生物物理学会年会, 2019年09月24日
20190924, 20190927

Progress of the protein neutron diffractometry to realize hydrogen high sensitivity analysis　　　　　　　　　　　　　　　
Ichiro Tanaka
日本生物物理学会年会, 2019年09月25日
20190924, 20190926

高感度水素検出による生体内化学反応の制御を目指して はじめに　　　　　　　　　　　　　　　
田中 伊知朗; 石北 央
日本生物物理学会年会, 2019年09月24日

タンパク質結晶解析へのDNPの応用とiMATERIA DNP-SANSへの期待　　　　　　　　　　　　　　　
新村 信雄、田中 伊知朗
ソフトマター中性子散乱研究会, 2019年08月21日, 茨城県中性子利用研究会, ［招待有り］
20190821, 20190821

Scope of the research base in Ibaraki University on the radiocesium emitted from Fukushima Daiichi Nuclear Power Plant　　　　　　　　　　　　　　　
Ichiro Tanaka
Ibaraki University-Institut de Radioprotection et de Surete Nucleaire (IRSN)/Japan-UK EICHI-project joint international workshop on radioactive particles, 2019年03月19日

福島第一原子力発電所事故由来の顆粒状放射性Csの可溶化について　　　　　　　　　　　　　　　
山口淳史、菊地賢司、佐伯夢、新村信雄、田中伊知朗
2018年度量子ビームサイエンスフェスタ, 2019年03月12日

放射性Csの存在様式を考慮した効果的で経済的な除染方法の開発　　　　　　　　　　　　　　　
佐伯 夢、田中 伊知朗
2018年度量子ビームサイエンスフェスタ, 2019年03月12日

リゾチーム加水分解反応機構の再解明に向けて　　　　　　　　　　　　　　　
後藤亮祐、田中伊知朗
2018年度量子ビームサイエンスフェスタ, 2019年03月12日

セリンプロテアーゼの反応速度制御と阻害剤複合体の中性子用大型結晶化　　　　　　　　　　　　　　　
杉山 玲、田中伊知朗
2018年度量子ビームサイエンスフェスタ, 2019年03月12日

大型タンパク質単結晶高圧凍結法の最適化　　　　　　　　　　　　　　　
青木 晃次、杉山玲、新井隆介、加藤康平、田中伊知朗
2018年度量子ビームサイエンスフェスタ, 2019年03月12日

中性子回折に向けたX線PF-BL17Aマイクロビームによる大型タンパク質単結晶の結晶品質評価　　　　　　　　　　　　　　　
新井 隆介、田中伊知朗
2018年度量子ビームサイエンスフェスタ, 2019年03月12日

DAPKタンパク質-ATPアナログ複合体の活性部位のX線構造解析とキナーゼ活性測定　　　　　　　　　　　　　　　
加藤 康平、田中伊知朗
2018年度量子ビームサイエンスフェスタ, 2019年03月12日

熱安定性による中性子回折用タンパク質良質大形結晶育成条件の探索　　　　　　　　　　　　　　　
西野宮 良太、田中伊知朗
2018年度量子ビームサイエンスフェスタ, 2019年03月12日

タンパク質中性子結晶解析に向けた核偏極用ドープ剤の影響　　　　　　　　　　　　　　　
小澤夏子、田中伊知朗
2018年度量子ビームサイエンスフェスタ, 2019年03月12日

大型良質タンパク質結晶育成のための微小空間での結晶育成制御　　　　　　　　　　　　　　　
佐藤允則; 田中伊知朗; 伊藤剛士; 真栄城正寿; 新村信雄
2018年度量子ビームサイエンスフェスタ, 2019年03月12日

How does granular radioactive Cs derived from the Fukushima Daiichi Nuclear Power Plant accident become soluble?　　　　　　　　　　　　　　　
Atsushi Yamaguchi; Kenji Kikuchi; Masakazu Komatsuzaki; Ichiro Tanaka; Yume Saeki; Nobuo Niimura
14th International Workshop on Spallation Materials Technology（IWSMT-14）, 2018年11月16日

Deuteration and IBARAKI Biological Crystal Diffractometer (iBIX)　　　　　　　　　　　　　　　
Ichiro Tanaka
Deuteration Workshop in the 3rd ESS-J-PARC Workshop, 2018年11月14日

中性子回折に向けたX線マイクロビームによる大型タンパク質単結晶の結晶品質評価　　　　　　　　　　　　　　　
新井隆介、田中伊知朗
日本結晶学会2018年会, 2018年11月10日

DAPKのキナーゼ活性と結晶構造との関係　　　　　　　　　　　　　　　
加藤康平、松尾悠平、田中伊知朗
第91回日本生化学会大会, 2018年09月26日

Optimization of high-pressure freezingand new radical doping for neutron protein crystallography(NPC) by dynamic nuclear polarization(DNP)　　　　　　　　　　　　　　　
Kouji Aoki; Ryusuke Arai; Kohei Kato; Rei Sugiyama; Ichiro Tanaka
第56回日本生物物理学会年会, 2018年09月15日

東海村J-PARCでの生命科学　　　　　　　　　　　　　　　
田中伊知朗
平成30年度ひたちなか市民大学, 2018年08月01日, 茨城県ひたちなか市, ［招待有り］

生体内分子の構造を見る　　　　　　　　　　　　　　　
田中伊知朗
平成30年度ひたちなか市民大学, 2018年07月18日, 茨城県ひたちなか市, ［招待有り］

Test measurement result and creation of large crystal for neutron structure analysis of lysozyme-glycoconjugate　　　　　　　　　　　　　　　
Ryosuke Goto; Katsuhiro Kusaka; Naomine Yano; Ichiro Tanaka
第18回蛋白質科学会年会, 2018年06月28日

Control of reaction rate of serine protease and X-ray crystal analysis of inhibitor complex　　　　　　　　　　　　　　　
Rei Sugiyama; Ichiro Tanaka
第3回茨城大学量子線科学国際シンポジウム, 2018年05月31日, 茨城大学大学院理工学研究科量子線科学専攻

Crystal quality evaluation of large protein single crystals by X-ray　　　　　　　　　　　　　　　
Ryusuke Arai; Kouzi Aoki; Saki Yamoto; Ichiro Tanaka
第3回茨城大学量子線科学国際シンポジウム, 2018年05月31日, 茨城大学大学院理工学研究科量子線科学専攻

X-ray analysis and kinase assay of DAPK protein-ATP analog complexs　　　　　　　　　　　　　　　
Kohei Kato; Yuhei Matuo; Ichiro Tanaka
第3回茨城大学量子線科学国際シンポジウム, 2018年05月31日, 茨城大学大学院理工学研究科量子線科学専攻

Large scale high quality crystal growth for neutron structure analysis of lysozyme-sugar complex　　　　　　　　　　　　　　　
Ryosuke Goto; Ichiro Tanaka
第3回茨城大学量子線科学国際シンポジウム, 2018年05月31日, 茨城大学大学院理工学研究科量子線科学専攻

Optimization of high-pressure freezing method of protein single crystals　　　　　　　　　　　　　　　
Kohji Aoki; Ryusuke Arai; Kouhei Kato; Rei Sugiyama; Saki Yamoto; Ichiro Tanaka
第3回茨城大学量子線科学国際シンポジウム, 2018年05月31日, 茨城大学大学院理工学研究科量子線科学専攻

研究部門：iBIX活用ユニット　　　　　　　　　　　　　　　
田中伊知朗
茨城大学フロンティア応用原子科学研究センター研究会, 2018年03月15日

Csの存在様式を考慮した福島原発由来土壌の除染に向けた試み　　　　　　　　　　　　　　　
坂本玲於奈、山口淳史、菊地賢司、新村信雄、田中伊知朗
2017年度量⼦ビームサイエンスフェスタ, 2018年03月04日

J-PARC MLFの第2ターゲットステーションに生物回折計を設置したら・・・　　　　　　　　　　　　　　　
田中伊知朗; 原田正英; 瀬戸秀紀
2017年度量⼦ビームサイエンスフェスタ, 2018年03月04日

DAPKタンパク質・ATPアナログ複合体のX線結晶解析とキナーゼ活性測定　　　　　　　　　　　　　　　
加藤康平、田中伊知朗
2017年度量⼦ビームサイエンスフェスタ, 2018年03月03日

タンパク質単結晶の高圧凍結法の最適化　　　　　　　　　　　　　　　
青木晃次、新井隆介、加藤康平、杉山玲、矢本早紀、田中伊知朗
2017年度量⼦ビームサイエンスフェスタ, 2018年03月03日

X線による大型タンパク質単結晶の結晶品質評価　　　　　　　　　　　　　　　
新井隆介、青木晃次、矢本早紀、田中伊知朗
2017年度量⼦ビームサイエンスフェスタ, 2018年03月03日

セリンプロテアーゼの反応速度制御と阻害剤複合体のX線結晶解析　　　　　　　　　　　　　　　
杉山玲、田中伊知朗
2017年度量⼦ビームサイエンスフェスタ, 2018年03月03日

リゾチーム-糖複合体の中性子構造解析に向けた大型良質結晶育成　　　　　　　　　　　　　　　
後藤亮祐、田中伊知朗
2017年度量⼦ビームサイエンスフェスタ, 2018年03月03日

グルコースイソメラーゼ‐グルコース複合体の中性子結晶構造解析　　　　　　　　　　　　　　　
矢本早紀、田中伊知朗
2017年度量⼦ビームサイエンスフェスタ, 2018年03月03日

J-PARC MLFの第2ターゲットステーションにおける生物回折計の検討　　　　　　　　　　　　　　　
田中伊知朗
第10回東海地区中性子生命科学検討会, 2018年02月28日

Search of the enzymatic reaction delay condition for reaction intermediate structure analysis　　　　　　　　　　　　　　　
杉山玲; 田中伊知朗
2017年度生命科学系学会合同年次大会, 2017年12月08日

MLF第2ターゲットステーションにおける 生物回折計の有効性の考察　　　　　　　　　　　　　　　
田中伊知朗
日本中性子科学会 第17回年会, 2017年12月03日

Lysozyme-糖複合体の中性子構造解析に向けた結晶育成　　　　　　　　　　　　　　　
後藤亮祐; 日下勝弘; 矢野直峰; 田中伊知朗
日本化学会関東支部茨城地区研究交流会, 2017年12月01日, 日本化学会関東支部

General Protonation Analysis of Histidines using 10 Neutron PDBs of Glucose Isomerase　　　　　　　　　　　　　　　
Masamichi Kimiyama; Ichiro Tanaka
International Conference on Neutron Scattering (ICNS2017), 2017年07月10日

Neutron protein crystallographic study of the glucose isomerization　　　　　　　　　　　　　　　
Saki Yamoto; Naoya Komatsuzaki; Katsuhiro Kusaka; Naomine Yano; Natsuki Okuda; Akio Sasaki; Ichiro Tanaka
International Conference on Neutron Scattering (ICNS2017), 2017年07月10日

General Protonation Analysis of Histidines using 10 Neutron PDBs ,of Glucose Isomerase　　　　　　　　　　　　　　　
Masamichi Kimiyama and *Ichiro Tanaka
International Conference on Neutron Scattering (ICNS2017), 2017年07月10日

Visualization of proton and electron transfer process of a biological reaction by μSR　　　　　　　　　　　　　　　
KIYOTANI, Tamiko; KOBAYASHI; Masayoshi; TANAKA, Ichiro; HIGEMOTO; WATARU; NIIMURA, Nobuo
The 14th International Conference on Muon Spin Rotation, Relaxation and Resonance, 2017年06月25日

Visualization of proton and electron transfer process of a,biological reaction by μSR　　　　　　　　　　　　　　　
KIYOTANI; Tamiko; KOBAYASHI; Masayoshi; TANAKA; Ichiro; HIGEMOTO; WATARU; NIIMURA; Nobuo
The 14th International Conference on,Muon Spin Rotation, Relaxation and Resonance, 2017年06月25日

福島原発由来不溶性放射性Csの溶解実験　　　　　　　　　　　　　　　
成田純、山口淳史、新村信雄、菊地賢司、小松崎将一; 田中伊知朗
2016年度量子ビームサイエンスフェスタ, 2017年03月14日

タンパク質の高圧凍結法の汎用化　　　　　　　　　　　　　　　
杉山玲; 小松崎直也; 後藤亮祐; 田中伊知朗
2016年度量子ビームサイエンスフェスタ, 2017年03月14日

リゾチーム－糖複合体の中性子構造解析に向けて　　　　　　　　　　　　　　　
後藤亮祐、日下勝弘; 矢野直峰; 田中伊知朗
2016年度量子ビームサイエンスフェスタ, 2017年03月14日

Glucose isomerase中性子座標データ10個を用いたヒスチジンのプロトネーション解析　　　　　　　　　　　　　　　
君山真陸、田中伊知朗
2016年度量子ビームサイエンスフェスタ, 2017年03月14日

ソーマチンの中性子結晶構造解析を目指した重水置換体のＸ線解析　　　　　　　　　　　　　　　
白川寛悟、田中伊知朗
2016年度量子ビームサイエンスフェスタ, 2017年03月14日

Glucose isomeraseの反応機構解明に向けた 中性子結晶構造解析　　　　　　　　　　　　　　　
矢本早紀; 小松崎直也; 日下勝弘; 矢野直峰; 奥田夏樹; 佐々木昭雄; 田中伊知朗
2016年度量子ビームサイエンスフェスタ, 2017年03月14日

DAPKキナーゼタンパク質とATP類似体複合体における結合様式の構造学的研究　　　　　　　　　　　　　　　
松尾悠平、田中伊知朗
2016年度量子ビームサイエンスフェスタ, 2017年03月14日

水素高感度検出に向けたタンパク質単結晶の動的核偏極と高圧凍結　　　　　　　　　　　　　　　
小松崎直也、田中伊知朗、岩田高弘、宮地義之、茶竹俊行、日下勝弘、新村信雄
2016年度量子ビームサイエンスフェスタ, 2017年03月14日

飛行時間法により収集されたタンパク質中性子回折データに対するプロファイルフィッティング法の適用　　　　　　　　　　　　　　　
矢野直峰、山田太郎、細谷孝明、大原高志、田中伊知郎、日下勝弘
2016年度量子ビームサイエンスフェスタ, 2017年03月14日

茨城県生命物質構造解析装置iBIX ー開発現状、成果及び今後の展望ー　　　　　　　　　　　　　　　
日下勝弘,山田太郎,矢野直峰,細谷孝明,大原高志,田中伊知朗,片桐政樹
2016年度量子ビームサイエンスフェスタ, 2017年03月14日

生体内で反応に関わるプロトンの高感度検出法の開発　　　　　　　　　　　　　　　
田中伊知朗
「水和とＡＴＰエネルギー」研究会, 2017年03月06日

タンパク質中性子結晶構造解析における動的核偏極による水素感度向上のための高圧凍結　　　　　　　　　　　　　　　
田中伊知朗、小松崎直也、岳文雪
日本中性子科学会年会, 2016年12月02日, 日本中性子科学会

Glucose isomeraseの中性子結晶構造解析による反応機構の解明に向けて　　　　　　　　　　　　　　　
矢本早紀; 小松崎直也; 日下勝弘; 矢野直峰; 奥田夏樹; 佐々木昭雄; 田中伊知朗
日本化学会関東支部茨城地区研究交流会, 2016年11月25日, 日本化学会関東支部

The preliminary result of Dynamic Nuclear Polarization method for more sensitive detection of hydrogen in Neutron Protein Crystallography　　　　　　　　　　　　　　　
Naoya Komatsuzaki; Ichiro Tanaka; Takahiro Iwata; Daisuke Miura; Yoshiyuki Miyachi; Genki Nukazuka; Hiroki Matsuda; Toshiyuki Chatake; Katsuhiro Kusaka; Nobuo Niimura
第54回日本生物物理学会年会, 2016年11月25日, 日本生物物理学会

ATP 類似化合物とDAPK 複合体における水和構造の解析　　　　　　　　　　　　　　　
松尾悠平、田中伊知朗
日本結晶学会年会, 2016年11月18日, 日本結晶学会

第169委員会補助 ISDSB2016報告　　　　　　　　　　　　　　　
田中伊知朗
回折構造生物 第169委員会 第51回研究会, 2016年11月08日, 回折構造生物 第169委員会

生体内反応に関与するタンパク質結晶解析のための水素核の動的核偏極　　　　　　　　　　　　　　　
三浦大輔; 岩田高広; 田中伊知郎; 宮地義之; 松田洋樹; 糠塚元気; 小松崎直也
日本物理学会年会, 2016年09月24日, 日本物理学会

Cryoprotectant-Free High-Pressure Freezing and Dynamic Nuclear Polarization for More Sensitive Detection of Hydrogen in Neutron Protein Crystallography (NPC) -One of improvement trials in NPC -　　　　　　　　　　　　　　　
Ichiro Tanaka; W.-X. Yue; N. Komatsuzaki; T. Chatake; K. Kusaka; N. Niimura; D. Miura; T. Iwata; Y. Miyachi; G. Nukaduka; H. Matsuda
Workshop for Quantum Beam Science held by iFRC, 2016年08月23日, 茨城大学フロンティアセンター

Cryoprotectant-Free High-Pressure Freezing and Dynamic Nuclear Polarization for More Sensitive Detection of Hydrogen in Neutron Protein Crystallography (NPC),-One of improvement trials in NPC -　　　　　　　　　　　　　　　
Ichiro Tanaka; W.-X. Yue; N. Komatsuzaki; T. Chatake; K. Kusaka; N. Niimura; D. Miura; T. Iwata; Y. Miyachi; G. Nukaduka; H. Matsuda
Workshop for Quantum Beam Science held by iFRC, 2016年08月23日, 茨城大学フロンティアセンター

Cryoprotectant-Free High-Pressure Freezing and Dynamic Nuclear Polarization for More Sensitive Detection of Hydrogen in Neutron Protein Crystallography (NPC) -One of improvement trials in NPC -　　　　　　　　　　　　　　　
Ichiro Tanaka; W.-X. Yue; N. Komatsuzaki; T. Chatake; K. Kusaka; N. Niimura; D. Miura; T. Iwata; Y. Miyachi; G. Nukaduka; H. Matsuda
The 5th Int’l Symposium for Diffraction Structural Biology(ISDSB2016), 2016年08月08日

Cryoprotectant-Free High-Pressure Freezing and Dynamic Nuclear Polarization for More Sensitive Detection of Hydrogen in Neutron Protein Crystallography (NPC),-One of improvement trials in NPC -　　　　　　　　　　　　　　　
Ichiro Tanaka; W.-X. Yue; N. Komatsuzaki; T. Chatake; K. Kusaka; N. Niimura; D. Miura; T. Iwata; Y. Miyachi; G. Nukaduka; H. Matsuda
The 5th Int’l Symposium for Diffraction Structural Biology(ISDSB2016), 2016年08月08日

生体内反応に関与する水素原子の高感度検出を目指して　　　　　　　　　　　　　　　
田中伊知朗
北里大学理学部セミナー, 2016年04月26日, 北里大学理学部, ［招待有り］

動的核偏極タンパク質中性子結晶解析のためのラジカル分子の導入とその評価　　　　　　　　　　　　　　　
小松崎 直也、田中 伊知朗、岩田 高広、宮地 義之
2015 年度量子ビームサイエンスフェスタ, 2016年03月15日

ソーマチンの甘味と構造に関する研究　　　　　　　　　　　　　　　
三ツ屋智弘、田中伊知朗
2015 年度量子ビームサイエンスフェスタ, 2016年03月15日

ATPおよび様々なATP類似体と結合したキナーゼタンパク質DAPKの構造比較　　　　　　　　　　　　　　　
松尾悠平、田中伊知朗
2015 年度量子ビームサイエンスフェスタ, 2016年03月15日

タンパク質単結晶の高圧凍結法の最適化　　　　　　　　　　　　　　　
岳文雪,飛田 雅之、田中伊知朗
2015 年度量子ビームサイエンスフェスタ, 2016年03月15日

糖- Lysozyme複合体の高分解能Ｘ線結晶構造解析　　　　　　　　　　　　　　　
嶋崎隼、田中伊知朗
2015 年度量子ビームサイエンスフェスタ, 2016年03月15日

多数のヨウ素イオンが配位したリゾチームタンパク質のX線構造解析　　　　　　　　　　　　　　　
小林政義、田中伊知朗
2015 年度量子ビームサイエンスフェスタ, 2016年03月15日

鉄貯蔵タンパク質アポフェリチンへFe2+イオンを導入したときの結晶学的研究　　　　　　　　　　　　　　　
矢本早紀、田中伊知朗
2015 年度量子ビームサイエンスフェスタ, 2016年03月15日

J-PARC およびPSI のμSR による酵素反応における電子とプロトン移動の可視化の予備的研究　　　　　　　　　　　　　　　
小林政義、清谷多美子、田中伊知朗、髭本亘、新村信雄
2015 年度量子ビームサイエンスフェスタ, 2016年03月15日

Visualization of electron and proton transfer process in an enzyme reaction by μSR (I)　　　　　　　　　　　　　　　
T. Kiyotani; M. Kobayashi; I. Tanaka; N. Niimura
International USMM&CMSI Workshop, 2016年01月06日

Visualization of electron and proton transfer process in an enzyme reaction by μSR (II)　　　　　　　　　　　　　　　
Masayoshi Kobayashi; Ichiro Tanaka; Tamiko Kiyotani; Wataru Higemoto; Nobuo Niimura
International USMM&CMSI Workshop, 2016年01月06日

水素高感度検出のためのラジカル分子の蛋白質結晶導入とその評価　　　　　　　　　　　　　　　
小松崎 直也、○田中 伊知朗
日本中性子科学会 第15回年会, 2015年12月11日, 日本中性子科学会

DAPKキナーゼタンパク質ATP類似体複合体における結合様式の構造学的研究　　　　　　　　　　　　　　　
松尾悠平; 山口淳史; 田中伊知朗
日本化学会関東支部茨城地区研究交流会, 2015年11月27日, 日本化学会関東支部

Neutron protein crystallography as the technique for not only the identification of protonation state but also function investigation　　　　　　　　　　　　　　　
Ichiro Tanaka
第53回日本生物物理学会年会シンポジウム, 2015年09月14日, 日本生物物理学会

An introduction of radical molecules into a protein single crystal for more sensitive detection of hydrogen in neutron crystallography　　　　　　　　　　　　　　　
Naoya Komatsuzaki; Takahiro Iwata; Yoshiyuki Miyachi; Toshiyuki Chatake; Katsuhiro Kusaka; Nobuo Niimura; Ichiro Tanaka
第53回日本生物物理学会年会, 2015年09月14日, 日本生物物理学会

生体高分子中性子結晶解析によるプロトネーション研究ー生体内反応に関与する水素原子ー　　　　　　　　　　　　　　　
田中伊知朗
新世代研究所2015年第1回水和ナノ構造研究会, 2015年09月01日, 新世代研究所水和ナノ構造研究会

タンパク質中性子結晶構造解析によるプロトン観測　　　　　　　　　　　　　　　
田中伊知朗、日下勝弘、山田太郎、細谷孝明、矢野直峰、片桐政樹、新村信雄、大原高志
膜タンパク質内部のプロトン透過を考える, 2015年04月20日, 分子研研究会

生体高分子中性子結晶構造解析によるプロトネーション研究のすゝめ　　　　　　　　　　　　　　　
田中伊知朗
日本物理学会, 2015年03月21日

中性子回折テストを含めたGlucose Isomeraseの結晶構造学的研究　　　　　　　　　　　　　　　
森一馬; 日下勝弘; 矢野直峰; 田中伊知朗
第3回物構研サイエンスフェスタ, 2015年03月17日

トリプシン酵素反応に伴う電子とプロトン移動の直接観察ためのμＳＲ実験　　　　　　　　　　　　　　　
小林政義; 田中伊知朗; 清谷多美子; 新村信雄
第3回物構研サイエンスフェスタ, 2015年03月17日

大形タンパク質単結晶を含めた高圧凍結法の最適化　　　　　　　　　　　　　　　
岳文雪、森一馬、田中伊知朗
第3回物構研サイエンスフェスタ, 2015年03月17日

核偏極中性子回折実験に向けたTEMPOL導入リゾチーム単結晶の準備とX線結晶構造解析　　　　　　　　　　　　　　　
小松崎 直也; 田中 伊知朗
第3回物構研サイエンスフェスタ, 2015年03月17日

強力な甘味タンパク質ソーマチンの中性および酸性pHでのX線結晶構造解析　　　　　　　　　　　　　　　
染谷穣児、田中伊知朗
第3回物構研サイエンスフェスタ, 2015年03月17日

キナーゼタンパク質DAPKと2種類のATP類似体複合体のX線結晶構造解析　　　　　　　　　　　　　　　
松尾悠平; 田中伊知朗
第3回物構研サイエンスフェスタ, 2015年03月17日

糖共存条件下でのリゾチームX線結晶構造解析　　　　　　　　　　　　　　　
松野公平、田中伊知朗
第3回物構研サイエンスフェスタ, 2015年03月17日

高圧凍結による大形タンパク質結晶の中性子実験に向けて　　　　　　　　　　　　　　　
岳文雪,田中伊知朗
日本結晶学会平成26年度年会, 2014年11月

NaIを沈殿剤としたリゾチームタンパク質のヨウ素配位　　　　　　　　　　　　　　　
Masayoshi Kobayashi; Ichiro Tanaka
第87回日本生化学会大会, 2014年10月17日

Towards the high-sensitive detection of hydrogen based on the proton polarization technique in neutron protein crystallography　　　　　　　　　　　　　　　
Ichiro Tanaka; Toshiyuki Chatake; Takahiro Iwata; Yoshiyuki Miyachi; Katsuhiro Kusaka; Nobuo Niimura
ICANS XXI: International Collaboration on Advanced Neutron Sources, 2014年09月30日

生体高分子中性子結晶構造解析におけるフーリエマップ改善のための実践的考察　　　　　　　　　　　　　　　
田中伊知朗、新村信雄
第52回日本生物物理学会年会, 2014年09月26日

中性子タンパク質結晶解析と水素・pKa・結晶育成新手法のよい関係　　　　　　　　　　　　　　　
田中伊知朗
新世代研究所2014年度第1回水和ナノ構造研究会, 2014年08月28日, 新世代研究所水和ナノ構造研究会

Radical doping and high-pressure freezing in an advanced neutron crystallography　　　　　　　　　　　　　　　
N. Morita; I. Tanaka; T. Chatake; S. Asaki; T. Iwat; K. Kusaka; N. Niimura
IUCr 2014, 2014年08月

Observation of electron transfer associated with enzymatic process by muSR　　　　　　　　　　　　　　　
T. Kiyotani; M. Kobayashi; I. Tanaka; N. Niimura
IUCr 2014, 2014年08月

Neutron diffraction study to elucidate reaction mechanism of RNase A　　　　　　　　　　　　　　　
K. Kusaka; T. Yamada; K. Tomoyori; T. Hosoya; T. Ohhara; I. Tanaka; N. Niimura
IUCr 2014, 2014年08月

Neutron crystallographic analysis of human α-thrombin using iBIX at J-PARC　　　　　　　　　　　　　　　
T. Yamada; K. Kusaka; T. Hosoya; T. Ohhara; K. Tomoyori; I. Tanaka; N. Niimura
IUCr 2014, 2014年08月

Neutron crystal structure of human FPPS complexed with risedronate　　　　　　　　　　　　　　　
T. Yokoyama; A. Ostermann; M. Mizuguchi; N. Niimura; T. Schrader; I. Tanaka
IUCr 2014, 2014年08月

Towards direct observation by μSR of electron transfer due to enzymatic reaction in trypsin　　　　　　　　　　　　　　　
Masayoshi Kobayashi; Ichiro Tanaka; Tamiko Kiyotani; Nobuo Niimura
The 2nd internation symposium on Science at J-PARC, 2014年07月14日

ATP-binding and hydration state analyses in DAPK towards neutron protein crystallography　　　　　　　　　　　　　　　
A. Yamaguchi; N. Niimura; S. Nakamura; S. Kidokoro; T. Chatake; T. Yokoyama; I. Tanaka
The 2nd internation symposium on Science at J-PARC, 2014年07月14日

生体水素水和水データベースを用いたタンパク質のプロトネーションおよび水和水の解析　　　　　　　　　　　　　　　
田中伊知朗、新村信雄
日本結晶学会平成25 年度年会, 2013年10月12日

J-PARCにおける生体高分子中性子結晶構造解析の進展　　　　　　　　　　　　　　　
Ichiro Tanaka
第86回日本生化学会大会, 2013年09月11日

IBARAKI Biological Crystal Diffractometer (iBIX) and towards the further structural biology　　　　　　　　　　　　　　　
Ichiro Tanaka
Eleventh International Topical Meeting on Nuclear Applications of Accelerators, (AppAcc13), 2013年08月06日

Fundamental studies for proton polarization technique in neutron protein crystallography　　　　　　　　　　　　　　　
I.Tanaka; K. Kusaka; T. Chatake; N. Niimura
4th International Symposium on Diffraction Structural Biology, 2013年05月27日

IBARAKI Biological Crystal Diffractometer (iBIX) at J-PARC　　　　　　　　　　　　　　　
Ichiro Tanaka
The 12th Korea-Japan Meeting on Neutron Science, 2013年02月04日

Diffractometers in Spallation Sources (iBIX）　　　　　　　　　　　　　　　
Ichiro Tanaka
Instrument Scientist Workshop on Single Crystal Neutron Diffraction Instruments, 2011年11月20日, 1st Asia-Oceania Conference on Neutron Scattering, ［招待有り］

Neutrons in diffraction structural biology making the best use of neutrons　　　　　　　　　　　　　　　
Ichiro Tanaka
3rd International Symposium on Diffraction Structural Biology (ISDSB 2010), 2010年05月28日, ［招待有り］

Overview of IBARAKI Biological Crystal Diffractometer (iBIX)　　　　　　　　　　　　　　　
Ichiro Tanaka
Neutrons in Biology 2009, 2009年10月26日, ［招待有り］

Initial Neutron Protein Diffraction Results at iBIX in J-PARC　　　　　　　　　　　　　　　
Ichiro Tanaka
International Conference on Neutron Scattering 2009(ICNS2009), 2009年05月05日, ［招待有り］

供用開始に際したJ-PARCの新しい生物用中性子回折装置（iBIX）　　　　　　　　　　　　　　　
田中伊知朗、日下勝弘、細谷孝明、新村信雄、大原高志、栗原和男、尾関智二
日本薬学会年会, 2009年03月27日, ［招待有り］

A new biological neutron diffractometer (iBIX) in J-PARC　　　　　　　　　　　　　　　
I. Tanaka; K. Kusaka; K. Tomoyori; N. Niimura; T. Ohhara; K. Kurihara; T. Hosoya; T. Ozeki
XXI Congress and General Assembly of the International Union of Crystallography (IUCr 2008), 2008年08月

Neutron protein crystallography in JRR-3 and future prospect in J-PARC　　　　　　　　　　　　　　　
Ichiro Tanaka
2nd International Symposium on Diffraction Structural Biology (ISDSB 2007), 2007年07月, ［招待有り］

Future Prospect of Neutron Protein Crystallography by Using New Spallation Neutron Sources　　　　　　　　　　　　　　　
Ichiro Tanaka
International Workshop on Advanced Jaue Diffraction in Frontier Science (Laue 2007), 2007年01月, ［招待有り］

新型生体高分子回折計（iBIX）の概要と化学・生命科学にもたらす新展開　　　　　　　　　　　　　　　
田中伊知朗、日下勝弘、友寄克亮、新村信雄、大原高志、栗原和男、細谷孝明、尾関智二
日本結晶学会年会, 2006年12月, ［招待有り］

IBARAKI Biological Crystal Diffractometer in J-PARC (BIX-P1)-General View-　　　　　　　　　　　　　　　
Ichiro Tanaka
American Crystallographic Society Annual Meeting, 2006年06月, ［招待有り］

日本生化学会

日本生物物理学会

日本結晶学会

日本中性子科学会

〔主要な業績〕中性子線を用いたタンパク質の動的な水和水の解析　　　　　　　　　　　　　　　
挑戦的研究（萌芽）
京都大学
2022年04月 - 2025年03月

〔主要な業績〕光をトリガとしない高速酵素反応機構解明
新学術領域（研究領域提案型）
茨城大学
2020年04月 - 2023年03月

〔主要な業績〕放射性Csの存在様式を意識した効果的で経済的な除染方法の開発　　　　　　　　　　　　　　　
挑戦的研究（萌芽）
2018年07月 - 2023年03月

量子ビームを用いた材料・生体の構造と機能の研究　　　　　　　　　　　　　　　
2010年04月 - 2014年03月

新型パルス中性子回折計を利用した次世代構造生物学
基盤研究(C)一般
茨城大学
2008年04月 - 2011年03月

２つの量子ビームを同時に利用した革新的な水素・水和構造情報獲得への挑戦
基盤研究(C)一般
茨城大学
2008年04月 - 2011年03月

New Methods of Bio-molecular Crystal Structure Determination Specific to Neutron Diffraction Data　　　　　　　　　　　　　　　
Human Frontier Science Program
2006年10月 - 2009年09月

中性子回折散乱実験技術AtoZ体験学習　　　　　　　　　　　　　　　
大学等連携支援事業
2008年04月 - 2009年03月

タンパク質のフォールディング、ダイナミクス及び分子認識に関与する水和構造
特定領域研究（公募）
茨城大学
2006年04月 - 2008年03月

生体物質の水素と水和水を含む新しい構造生物化学の構築
基盤研究(B)一般
茨城大学
2005年04月 - 2008年03月

タンパク質のフォールディングやダイナミクスに関する水和構造
特定領域研究（公募）
茨城大学
2004年04月 - 2006年03月

水素・水和構造を含めた新しい構造生物学の開拓　　　　　　　　　　　　　　　
科学技術振興調整費
1999年10月 - 2004年03月

特開2022-087076, 特願2021-193746, マイクロ流路デバイスを用いた結晶製造方法及び装置
田中伊知朗、長谷川智紀、新村信雄、齋藤洋也(茨城大学), 山田貢、石田卓也、吉崎泉(JAXA), 皆川由貴、伊藤剛士((株)化研), 真栄城正寿(北海道大学)

特開2002-323726, 特願2001-127394, 放射線画像読取装置