WEKO3
アイテム
High-resolution neutron crystal structural studies of electron transfer proteins
https://repo.qst.go.jp/records/65961
https://repo.qst.go.jp/records/6596100ec4d2b-f135-439e-a04b-9e9c6d77f64f
| Item type | 会議発表用資料 / Presentation(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2016-09-20 | |||||
| タイトル | ||||||
| タイトル | High-resolution neutron crystal structural studies of electron transfer proteins | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_c94f | |||||
| 資源タイプ | conference object | |||||
| アクセス権 | ||||||
| アクセス権 | metadata only access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
| 著者 |
玉田, 太郎
× 玉田, 太郎× 玉田 太郎 |
|||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | 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). | |||||
| 会議概要（会議名, 開催地, 会期, 主催者等） | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | IPR International Symposium, 2016 Taiwan-Japan Joint Symposium of Crystallography | |||||
| 発表年月日 | ||||||
| 日付 | 2016-06-23 | |||||
| 日付タイプ | Issued | |||||
