| Literature DB >> 32093829 |
Ichiro Tanaka1, Toshiyuki Chatake2, Satoru Fujiwara3, Takaaki Hosoya4, Katsuhiro Kusaka5, Nobuo Niimura5, Taro Yamada5, Naomine Yano5.
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.Entities:
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
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Year: 2020 PMID： 32093829 DOI： 10.1016/bs.mie.2020.01.002
Source DB: PubMed Journal: Methods Enzymol ISSN： 0076-6879 Impact factor: 1.600