Fast native-SAD phasing for routine macromolecular structure determination

Weinert Tobias; Olieric Vincent; Waltersperger Sandro; Panepucci Ezequiel; Chen Lirong; Zhang Hua; Zhou Dayong; Rose John; Ebihara Akio; Kuramitsu Seiki; Li Dianfan; Howe Nicole; Schnapp Gisela; Pautsch Alexander; Bargsten Katja; Prota Andrea E; Surana Parag; Kottur Jithesh; Nair Deepak T; Basilico Federica; Cecatiello Valentina; Pasqualato Sebastiano; Boland Andreas; Weichenrieder Oliver; Wang Bi Cheng; Steinmetz Michel O; Caffrey Martin; Wang Meitian<sup>*</sup>

doi:10.1038/nmeth.3211

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Fast native-SAD phasing for routine macromolecular structure determination

作者：Weinert Tobias; Olieric Vincent; Waltersperger Sandro; Panepucci Ezequiel; Chen Lirong; Zhang Hua; Zhou Dayong; Rose John; Ebihara Akio; Kuramitsu Seiki; Li Dianfan; Howe Nicole; Schnapp Gisela; Pautsch Alexander; Bargsten Katja; Prota Andrea E; Surana Parag; Kottur Jithesh; Nair Deepak T; Basilico Federica; Cecatiello Valentina; Pasqualato Sebastiano; Boland Andreas; Weichenrieder Oliver; Wang Bi Cheng; Steinmetz Michel O; Caffrey Martin; Wang Meitian^*

来源：Nature Methods, 2015, 12(2): 131-U163.

DOI：10.1038/nmeth.3211

摘要

We describe a data collection method that uses a single crystal to solve X-ray structures by native SAD (single-wavelength anomalous diffraction). We solved the structures of 11 real-life examples, including a human membrane protein, a protein-DNA complex and a 266-kDa multiprotein-ligand complex, using this method. The data collection strategy is suitable for routine structure determination and can be implemented at most macromolecular crystallography synchrotron beamlines.