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Experimental phase determination with selenomethionine or mercury-derivatization in serial femtosecond crystallography

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 previ...

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Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5619855/
https://www.ncbi.nlm.nih.gov/pubmed/28989719
http://dx.doi.org/10.1107/S2052252517008557
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author 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
author_facet 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
author_sort Yamashita, Keitaro
collection PubMed
description 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.
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spelling pubmed-56198552017-10-06 Experimental phase determination with selenomethionine or mercury-derivatization in serial femtosecond crystallography 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 IUCrJ Research Papers 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. International Union of Crystallography 2017-08-08 /pmc/articles/PMC5619855/ /pubmed/28989719 http://dx.doi.org/10.1107/S2052252517008557 Text en © Keitaro Yamashita et al. 2017 http://creativecommons.org/licenses/by/2.0/uk/ 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.http://creativecommons.org/licenses/by/2.0/uk/
spellingShingle Research Papers
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
Experimental phase determination with selenomethionine or mercury-derivatization in serial femtosecond crystallography
title Experimental phase determination with selenomethionine or mercury-derivatization in serial femtosecond crystallography
title_full Experimental phase determination with selenomethionine or mercury-derivatization in serial femtosecond crystallography
title_fullStr Experimental phase determination with selenomethionine or mercury-derivatization in serial femtosecond crystallography
title_full_unstemmed Experimental phase determination with selenomethionine or mercury-derivatization in serial femtosecond crystallography
title_short Experimental phase determination with selenomethionine or mercury-derivatization in serial femtosecond crystallography
title_sort experimental phase determination with selenomethionine or mercury-derivatization in serial femtosecond crystallography
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5619855/
https://www.ncbi.nlm.nih.gov/pubmed/28989719
http://dx.doi.org/10.1107/S2052252517008557
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