| Literature DB >> 25506719 |
Tobias Weinert1, Vincent Olieric1, Sandro Waltersperger1, Ezequiel Panepucci1, Lirong Chen2, Hua Zhang2, Dayong Zhou2, John Rose2, Akio Ebihara3, Seiki Kuramitsu4, Dianfan Li5, Nicole Howe5, Gisela Schnapp6, Alexander Pautsch6, Katja Bargsten7, Andrea E Prota7, Parag Surana8, Jithesh Kottur8, Deepak T Nair8, Federica Basilico9, Valentina Cecatiello9, Sebastiano Pasqualato9, Andreas Boland10, Oliver Weichenrieder10, Bi-Cheng Wang2, Michel O Steinmetz7, Martin Caffrey5, Meitian Wang1.
Abstract
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.Entities:
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Year: 2014 PMID： 25506719 DOI： 10.1038/nmeth.3211
Source DB: PubMed Journal: Nat Methods ISSN： 1548-7091 Impact factor: 28.547