@misc{oai:repo.qst.go.jp:00073076,
 author = {平野, 優 and 栗原, 和男 and Ostermann, Andreas and Kusaka, Katsuhiro and Kimura, Shigenobu and Miki, Kunio and 玉田, 太郎 and 平野 優 and 栗原 和男 and 玉田 太郎},
 month = {Dec},
 note = {Many redox proteins possess cofactors, such as heme, FAD, and Fe-S cluster and the cofactors are involved in the chemical reactions of redox proteins. The redox reactions in proteins usually associate with the movement of hydrogen atoms and/or valence electrons through the cofactors. High-resolution neutron and X-ray structure analyses can provide the information about hydrogen atoms and valence electrons and are important for understanding molecular mechanisms of redox reactions in proteins. NADH-cytochrome b5 reductase (b5R) catalyzes the electron transfer from two-electron carriers of NADH to one-electron acceptor of cytochrome b5 (b5). High-resolution X-ray structure analyses have been reported for b5R and b5 from porcine liver. We prepared large crystals (> 1mm3) of the oxidized form of b5R for neutron diffraction experiments in the different pH conditions (6.5 and 7.5). We have successfully collected neutron diffraction data sets at high-resolutions of 1.40 Å (at iBIX in J-PARC) and 1.45 Å (at BIODIFF in FRM II). The diffraction data sets of iBIX were collected by the TOF-Laue method which utilizes white-pulsed neutrons. The integrated intensities of the iBIX data were corrected by applying wavelength normalization. The neutron structures obtained in different pH conditions show small structural changes in the hydrogen-bond network from FAD to the protein surface., Asian Crystallographic Association Conference 2018},
 title = {Neutron crystal structure studies of the oxidized form of NADH-cytochrome b5 reductase},
 year = {2018}
}