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

Fast native-SAD phasing for routine macromolecular structure determination.

Author information

1
Swiss Light Source at Paul Scherrer Institut, Villigen, Switzerland.
2
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA.
3
Laboratory of Biological Chemistry, Faculty of Applied Biological Sciences, Gifu University, Gifu, Japan.
4
Department of Biological Sciences, Graduate School of Science, Osaka University, Osaka, Japan.
5
Membrane Structural and Functional Biology Group, School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland.
6
Boehringer Ingelheim Pharma GmbH and Co. KG, Biberach an der Riss, Germany.
7
Laboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institut, Villigen, Switzerland.
8
National Centre for Biological Sciences, Bangalore, India.
9
Department of Experimental Oncology, European Institute of Oncology, Milan, Italy.
10
Department of Biochemistry, Max Planck Institute for Developmental Biology, Tübingen, Germany.

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.

PMID:
25506719
DOI:
10.1038/nmeth.3211
[Indexed for MEDLINE]
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