Ionic radii in fluorites

Vauchy, R.; Hirooka, Shun; Murakami, Tatsutoshi

Materialia, 32, p.101934_1 - 101934_12, 2023/12

https://doi.org/10.1016/j.mtla.2023.101934

Cesium chemisorbed species onto stainless steel surfaces; An Atomistic scale study

Miradji, F.; Suzuki, Chikashi; Nakajima, Kunihisa; Osaka, Masahiko

Journal of Physics and Chemistry of Solids, 136, p.109168_1 - 109168_9, 2020/01

https://doi.org/10.1016/j.jpcs.2019.109168

A Neutron crystallographic analysis of a rubredoxin mutant at 1.6 resolution

Chatake, Toshiyuki*; Kurihara, Kazuo; Tanaka, Ichiro*; Tsyba, I.*; Bau, R.*; Jenney, F. E. Jr.*; Adams, M. W. W.*; Niimura, Nobuo

Acta Crystallographica Section D, 60(8), p.1364 - 1373, 2004/08

https://doi.org/10.1107/S090744490401176X

A neutron diffraction study has been carried out at 1.6 resolution on a mutant rubredoxin from using the BIX-3 single-crystal diffractometer at the JRR-3 reactor of JAERI. In order to study the unusual thermostability of rubredoxin from , the hydrogen-bonding patterns were compared between the native and a 'triple-mutant' variant where three residues were changed so that they are identical to those in a mesophilic rubredoxin. 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. The H/D-exchange ratios in the protein were also studied. The results suggest that the backbone amide bonds near the four Cys residues of the FeS redox center are most resistant to H/D exchange. In addition, the 1.6 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.

Neutron diffractometer for biological macromolecule crystallography

Kurihara, Kazuo; Tanaka, Ichiro*; Niimura, Nobuo

Nihon Kessho Gakkai-Shi, 46(3), p.193 - 200, 2004/05

https://doi.org/10.5940/jcrsj.46.193

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.

A High-performance neutron diffractometer for biological crystallography (BIX-3)

Tanaka, Ichiro; Kurihara, Kazuo; Chatake, Toshiyuki; Niimura, Nobuo

Journal of Applied Crystallography, 35(Part1), p.34 - 40, 2002/02

A high performance neutron diffractometer for biological crystallography (BIX-3) has been constructed at JRR-3M in Japan Atomic Energy Research Institute (JAERI) in order to determine the hydrogen positions in biological macromolecules. It uses several recent technical innovations, such as a neutron imaging plate and an elastically bent silicon monochromator developed by the authors. These have made it possible to realize a compact vertical arrangement of the diffractometer. Diffraction data have been collected from the proteins rubredoxin and myoglobin in about one month, to a resolution of 1.5, good enough to identify the hydrogen atoms with high accuracy. By adopting a crystal-step scan method for measuring Bragg diffraction intensities, the signal to noise ratio was much better than that of the Laue method. This shows that BIX-3 is one of the best-performing machines for neutron protein crystallography in the world currently.

Neutron diffraction study on the structure of rubredoxin from it Pyrococcus furiosus

Kurihara, Kazuo; Tanaka, Ichiro; Adams, M. W. W.*; Jenney, F. E. Jr.*; Moiseeva, N.*; Bau, R.*; Niimura, Nobuo

Journal of the Physical Society of Japan, Vol.70, Supplement A, p.400 - 402, 2001/05

With the new single-crystal diffractometer BIX-3 at the JRR-3M reactor of JAERI, a single-crystal neutron diffraction analysis of the structure of the small protein rubredoxin from the hyperthermophile Pyrococcus furiosus is currently under way. Data were collected at room temperature up to a resolution of 1.5 intervals in and exposure times ranging from 60 to 77 minutes per frame. The completeness factor of the 1.5-. Included in the refinement are 301 hydrogen atoms and 40 deuterium atoms, and 29 water molecules were also identified. In the present model, the current value for R and R are 24.0 and 26.3 , respectively.

Crystallographic study on the phase transition of -UN

Serizawa, Hiroyuki; Fukuda, Kosaku; *

Transactions of the American Nuclear Society, 66, p.196 - 197, 1992/11

no abstracts in English

Structural and thermal properties of Cs-Fe-Si-O systems under LWR severe accident by DFT calculations

Miradji, F.; Suzuki, Chikashi; Nakajima, Kunihisa; Osaka, Masahiko

no journal, , 

Neutron diffractometer for protein crystallography at cold neutron beam line of JRR-3

Kurihara, Kazuo*; Tamura, Itaru; Hirano, Yu*; Hiromoto, Takeshi*; Kono, Fumiaki*; Tamada, Taro*

no journal, ,