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Oral presentation

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

Tamada, Taro; Hirano, Yu; Tomoyori, Katsuaki; Kurihara, Kazuo

no journal, , 

Two facilities for neutron protein crystallography have been installed in Japan Atomic Energy Agency. One is the research reactor, JRR-3, and the other is Material and Life science experimental Facility (MLF) in J-PARC. We have performed high-resolution neutron crystal structure analyses of two electron transfer proteins. We succeeded in data collection of these proteins at higher resolution, 1.1${AA}$ (high-potential iron-sulfur protein) and 1.4${AA}$ (NADH-cytochrome b5 reductase), using BL03 (iBIX) beamline in J-PARC/MLF. Joint neutron and X-ray crystallographic refinement is in progress, but we have already confirmed some characteristic hydorogens which have unideal geometries. In addition, we have a plan of installation of new diffractomer in J-PARC, which is able to cover such a crystal with large unit cell (~250${AA}$). The operation of new diffractometer will allow neutron structure analyses of membrane proteins and protein complexes. In this presentation, we also talk about our approach for installation of new diffractomer.

Oral presentation

Structure of hydrogen atoms in high-resolution neutron structure of protein

Hirano, Yu; Tamada, Taro; Kurihara, Kazuo; Kusaka, Katsuhiro*; Ono, Hiraku*; Takeda, Kazuki*; Miki, Kunio*

no journal, , 

Hydrogen atoms are involved in protein folding and enzymatic reaction. Structures of hydrogen atoms in proteins have been discussed based on the ideal bond distances and angles obtained by small molecular crystallography. However, structural information about hydrogen atoms without geometric restraints is important for understanding structures and functions of proteins. High-potential iron-sulfur protein (HiPIP) is an electron carrier protein which functions in photosynthetic electron transfer chain of purple bacteria. In this work, we determined high-resolution neutron structure of HiPIP. The neutron diffraction experiment was performed at the BL03 beamline (iBIX) of J-PARC/MLF. We have collected the highest resolution data at 1.1 angstrom in the protein neutron structures. After structure refinement, we have observed many deviations in positions and bond lengths of hydrogen atoms from the ideal geometries.

Oral presentation

Neutron structure determination of perdeuterated T4 phage lysozyme

Hiromoto, Takeshi; Shimizu, Rumi; Adachi, Motoyasu; Shibazaki, Chie; Kuroki, Ryota

no journal, , 

no abstracts in English

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