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Title: Experimental phase determination with selenomethionine or mercury-derivatization in serial femtosecond crystallography
Authors: Yamashita, Keitaro
Kuwabara, Naoyuki
Nakane, Takanori
Murai, Tomohiro
Mizohata, Eiichi
Sugahara, Michihiro
Pan, Dongqing  kyouindb  KAKEN_id  orcid (unconfirmed)
Masuda, Tetsuya  kyouindb  KAKEN_id  orcid (unconfirmed)
Suzuki, Mamoru
Sato, Tomomi
Kodan, Atsushi  kyouindb  KAKEN_id  orcid (unconfirmed)
Yamaguchi, Tomohiro  kyouindb  KAKEN_id
Nango, Eriko  kyouindb  KAKEN_id
Tanaka, Tomoyuki
Tono, Kensuke
Joti, Yasumasa
Kameshima, Takashi
Hatsui, Takaki
Yabashi, Makina
Manya, Hiroshi
Endo, Tamao
Kato, Ryuichi
Senda, Toshiya
Kato, Hiroaki  kyouindb  KAKEN_id  orcid (unconfirmed)
Iwata, So  kyouindb  KAKEN_id
Ago, Hideo
Yamamoto, Masaki
Yumoto, Fumiaki
Nakatsu, Toru  kyouindb  KAKEN_id  orcid (unconfirmed)
Author's alias: 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
Keywords: serial femtosecond crystallography
SAD phasing
selenomethionine derivatization
mercury soaking
Issue Date: Sep-2017
Publisher: International Union of Crystallography (IUCr)
Journal title: IUCrJ
Volume: 4
Issue: 5
Start page: 639
End page: 647
Abstract: 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.
Description: 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.
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.
DOI(Published Version): 10.1107/S2052252517008557
PubMed ID: 28989719
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