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Current status and near future plan of neutron protein crystallography at J-PARC.
Tanaka, Ichiro; Chatake, Toshiyuki; Fujiwara, Satoru; Hosoya, Takaaki; Kusaka, Katsuhiro; Niimura, Nobuo; Yamada, Taro; Yano, Naomine.
Afiliação
  • Tanaka I; Domain of Materials Science and Engineering, Graduate School of Science and Engineering, Ibaraki University, Hitachi, Ibaraki, Japan; Divisions of Neutron Beamline and Research, Frontier Research Center for Applied Atomic Sciences, Tokai, Ibaraki, Japan. Electronic address: ichiro.tanaka.h27@vc.ibar
  • Chatake T; Institute for Integrated Radiation and Nuclear Science, Kyoto University, Kumatori, Osaka, Japan.
  • Fujiwara S; Institute for Quantum Life Science, National Institutes for Quantum and Radiological Science and Technology, Tokai, Ibaraki, Japan.
  • Hosoya T; Domain of Materials Science and Engineering, Graduate School of Science and Engineering, Ibaraki University, Hitachi, Ibaraki, Japan; Divisions of Neutron Beamline and Research, Frontier Research Center for Applied Atomic Sciences, Tokai, Ibaraki, Japan.
  • Kusaka K; Divisions of Neutron Beamline and Research, Frontier Research Center for Applied Atomic Sciences, Tokai, Ibaraki, Japan.
  • Niimura N; Divisions of Neutron Beamline and Research, Frontier Research Center for Applied Atomic Sciences, Tokai, Ibaraki, Japan.
  • Yamada T; Divisions of Neutron Beamline and Research, Frontier Research Center for Applied Atomic Sciences, Tokai, Ibaraki, Japan.
  • Yano N; Divisions of Neutron Beamline and Research, Frontier Research Center for Applied Atomic Sciences, Tokai, Ibaraki, Japan.
Methods Enzymol ; 634: 101-123, 2020.
Article em En | MEDLINE | ID: mdl-32093829
ABSTRACT
The IBARAKI Biological Crystal Diffractometer (iBIX) has been available for use at MLF (Material and Life Science Facility) in J-PARC (Japan Proton Accelerator Research Complex) since 2008. The development in state-of-the-art detector systems could enable iBIX to become one of the highest-performance neutron single-crystal diffractometers in the world. Here, together with other various developments, such as data reduction software, crystal growth, and new techniques in measurement coupled analysis, we provided new hydrogen and water structural data of several proteins and macromolecules. Although the proton power at MLF has not yet reached its planned maximum (1MW), a more powerful neutron source will be soon needed for neutron protein crystallography. A future idea is also proposed and discussed in this article.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas / Difração de Nêutrons Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas / Difração de Nêutrons Idioma: En Ano de publicação: 2020 Tipo de documento: Article