التفاصيل البيبلوغرافية
| العنوان: |
Experimental phase determination with selenomethionine or mercury-derivatization in serial femtosecond crystallography |
| المؤلفون: |
Yamashita, Keitaro, Kuwabara, Naoyuki, Nakane, Takanori, Murai, Tomohiro, Mizohata, Eiichi, Sugahara, Michihiro, Pan, Dongqing, Masuda, Tetsuya, Suzuki, Mamoru, Sato, Tomomi, Kodan, Atsushi, Yamaguchi, Tomohiro, Nango, Eriko, Tanaka, Tomoyuki, Tono, Kensuke, Joti, Yasumasa, Kameshima, Takashi, Hatsui, Takaki, Yabashi, Makina, Manya, Hiroshi, Endo, Tamao, Kato, Ryuichi, Senda, Toshiya, Kato, Hiroaki, Iwata, So, Ago, Hideo, Yamamoto, Masaki, Yumoto, Fumiaki, Nakatsu, Toru |
| المساهمون: |
山下, 恵太郎, 桑原, 直之, 中根, 崇智, 村井, 智洋, 溝端, 栄一, 潘, 東青, 鈴木, 守, 登野, 健介, 加藤, 博章, 岩田, 想, 湯本, 史明, 中津, 亨, 50710787, 80311744, 80360543, 80346791, 90376947, 90204487, 60452330, 50293949 |
| بيانات النشر: |
International Union of Crystallography (IUCr) |
| سنة النشر: |
2017 |
| المجموعة: |
Kyoto University Research Information Repository (KURENAI) / 京都大学学術情報リポジトリ |
| مصطلحات موضوعية: |
serial femtosecond crystallography, SAD phasing, XFELs, selenomethionine derivatization, mercury soaking |
| الوصف: |
SACLAの得意とするX線波長でタンパク質微結晶の新規構造解析に成功. 京都大学プレスリリース. 2017-08-23. ; Serial femtosecond crystallography (SFX) using X-ray free-electron lasers (XFELs) holds enormous potential for the structure determination of proteins for which it is difficult to produce large and high-quality crystals. SFX has been applied to various systems, but rarely to proteins that have previously unknown structures. Consequently, the majority of previously obtained SFX structures have been solved by the molecular replacement method. To facilitate protein structure determination by SFX, it is essential to establish phasing methods that work efficiently for SFX. Here, selenomethionine derivatization and mercury soaking have been investigated for SFX experiments using the high-energy XFEL at the SPring-8 Angstrom Compact Free-Electron Laser (SACLA), Hyogo, Japan. Three successful cases are reported of single-wavelength anomalous diffraction (SAD) phasing using X-rays of less than 1 Å wavelength with reasonable numbers of diffraction patterns (13 000, 60 000 and 11 000). It is demonstrated that the combination of high-energy X-rays from an XFEL and commonly used heavy-atom incorporation techniques will enable routine de novo structural determination of biomacromolecules. |
| نوع الوثيقة: |
article in journal/newspaper |
| وصف الملف: |
application/pdf |
| اللغة: |
English |
| تدمد: |
2052-2525 |
| Relation: |
http://www.kyoto-u.ac.jp/ja/research/research_results/2017/170810_2.html; http://hdl.handle.net/2433/226830; IUCrJ; 639; 647 |
| الاتاحة: |
http://hdl.handle.net/2433/226830 |
| Rights: |
This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
| رقم الانضمام: |
edsbas.FC9D2172 |
| قاعدة البيانات: |
BASE |
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