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. 2015 Feb;12(2):131-3.
doi: 10.1038/nmeth.3211. Epub 2014 Dec 15.

Fast native-SAD phasing for routine macromolecular structure determination

Tobias Weinert  1 , Vincent Olieric  1 , Sandro Waltersperger  1 , Ezequiel Panepucci  1 , Lirong Chen  2 , Hua Zhang  2 , Dayong Zhou  2 , John Rose  2 , Akio Ebihara  3 , Seiki Kuramitsu  4 , Dianfan Li  5 , Nicole Howe  5 , Gisela Schnapp  6 , Alexander Pautsch  6 , Katja Bargsten  7 , Andrea E Prota  7 , Parag Surana  8 , Jithesh Kottur  8 , Deepak T Nair  8 , Federica Basilico  9 , Valentina Cecatiello  9 , Sebastiano Pasqualato  9 , Andreas Boland  10 , Oliver Weichenrieder  10 , Bi-Cheng Wang  2 , Michel O Steinmetz  7 , Martin Caffrey  5 , Meitian Wang  1
Affiliations

Fast native-SAD phasing for routine macromolecular structure determination

Tobias Weinert et al. Nat Methods. 2015 Feb.

Erratum in

  • Nat Methods. 2015 Jul;12(7):692

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.

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