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Journal Articles

Structure analysis and derivation of deformed electron density distribution of polydiacetylene giant single crystal by the combination of X-ray and neutron diffraction data

Tashiro, Koji*; Kusaka, Katsuhiro*; Hosoya, Takaaki*; Ohara, Takashi; Hanesaka, Makoto*; Yoshizawa, Yoshinori*; Yamamoto, Hiroko*; Niimura, Nobuo*; Tanaka, Ichiro*; Kurihara, Kazuo*; et al.

Macromolecules, 51(11), p.3911 - 3922, 2018/06

 Times Cited Count:4 Percentile:14.91(Polymer Science)

Journal Articles

A Neutron crystallographic analysis of a rubredoxin mutant at 1.6 ${AA}$ 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

 Times Cited Count:33 Percentile:89.35(Biochemical Research Methods)

A neutron diffraction study has been carried out at 1.6 ${AA}$ resolution on a mutant rubredoxin from ${it Pyrococcus furiosus}$ using the BIX-3 single-crystal diffractometer at the JRR-3 reactor of JAERI. In order to study the unusual thermostability of rubredoxin from ${it P. furiosus}$, 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$$_{4}$$ redox center are most resistant to H/D exchange. In addition, the 1.6 ${AA}$ 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.

Journal Articles

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 $AA (the highest resolution obtained thus far for a neutron data set). Data collection was by the step-scan method, with 0.3$^o$$ intervals in $$phi$$ and exposure times ranging from 60 to 77 minutes per frame. The completeness factor of the 1.5-$AA resolution data set is currently at 76.8 $%$$. 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$$_free$$ are 24.0 $$%$$ and 26.3 $$%$$, respectively.

Oral presentation

Upgrading of diffractometer for protein crystallography, BIX-3,4

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

no journal, , 

no abstracts in English

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