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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...
Autores principales: | , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2017
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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. |
format | Online Article Text |
id | pubmed-5619855 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
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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