Fast native-SAD phasing for routine macromolecular structure determination

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

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)131-133
Number of pages3
JournalNature Methods
Volume12
Issue number2
DOIs
Publication statusPublished - Jan 1 2015

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Biology
  • Biochemistry
  • Cell Biology
  • Medicine(all)

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