Current status and near future plan of neutron protein crystallography at J-PARC

Ichiro Tanaka; Toshiyuki Chatake; Satoru Fujiwara; Takaaki Hosoya; Katsuhiro Kusaka; Nobuo Niimura; Taro Yamada; Naomine Yano

doi:10.1016/bs.mie.2020.01.002

Current status and near future plan of neutron protein crystallography at J-PARC

Methods Enzymol. 2020:634:101-123. doi: 10.1016/bs.mie.2020.01.002. Epub 2020 Feb 8.

Authors

Ichiro Tanaka¹, Toshiyuki Chatake², Satoru Fujiwara³, Takaaki Hosoya⁴, Katsuhiro Kusaka⁵, Nobuo Niimura⁵, Taro Yamada⁵, Naomine Yano⁵

Affiliations

¹ 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.ibaraki.ac.jp.
² Institute for Integrated Radiation and Nuclear Science, Kyoto University, Kumatori, Osaka, Japan.
³ Institute for Quantum Life Science, National Institutes for Quantum and Radiological Science and Technology, Tokai, Ibaraki, Japan.
⁴ 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.
⁵ Divisions of Neutron Beamline and Research, Frontier Research Center for Applied Atomic Sciences, Tokai, Ibaraki, Japan.

PMID: 32093829
DOI: 10.1016/bs.mie.2020.01.002

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.

Keywords: D/H contrast neutron crystallography; Data processing; Detector; Dynamic nuclear polarization; High-pressure freezing; IBARAKI biological crystal diffractometer (iBIX); Large protein crystal growth; Second target station; Structure refinement.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallization
Crystallography
Crystallography, X-Ray
Neutron Diffraction*
Neutrons
Proteins*

Substances

Proteins