Scientific article
English

Fast native-SAD phasing for routine macromolecular structure determination

Published inNature methods, vol. 12, no. 2, p. 131-133
Publication date2015-02-06
First online date2014-12-15
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.

Affiliation entities Not a UNIGE publication
Citation (ISO format)
WEINERT, Tobias et al. Fast native-SAD phasing for routine macromolecular structure determination. In: Nature methods, 2015, vol. 12, n° 2, p. 131–133. doi: 10.1038/nmeth.3211
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Additional URL for this publicationhttps://www.nature.com/articles/nmeth.3211
Journal ISSN1548-7091
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