@misc{oai:repo.qst.go.jp:00065961,
 author = {玉田, 太郎 and 玉田 太郎},
 month = {Jun},
 note = {Neutron crystallography is a powerful technique to obtain accurate positions of hydrogen atoms in protein structures. Recently, we have performed high-resolution neutron crystal structure analyses of high-potential iron-sulfur protein (HiPIP) and NADH-cytochrome b5 reductase (b5R). We succeeded in data collection of these proteins at higher resolution, 1.1 Å (HiPIP) and 1.4 Å (b5R), using pulsed neutron beams at BL03 (iBIX) beamline in MLF/J-PARC. Joint neutron and X-ray crystallographic refinement is in progress, but we have already observed protonation statuses of polar residues located in molecular surface and orientation of water molecules. Furthermore, we confirmed some characteristic hydorogens which have unideal geometries. In this presentation, I also talk about our plan of new diffractomer in J-PARC, which is able to cover such a crystal with large unit cell (~ 250 Å)., IPR International Symposium, 2016 Taiwan-Japan Joint Symposium of Crystallography},
 title = {High-resolution neutron crystal structural studies of electron transfer proteins},
 year = {2016}
}