Fast native-SAD phasing for routine macromolecular structure determination

Weinert, T; Olieric, V; Waltersperger, S; Panepucci, E; Chen, L; Zhang, H; Zhou, D; Rose, J; Ebihara, A; Kuramitsu, S; Li, D; Howe, N; Schnapp, G; Pautsch, A; Bargsten, K; Prota, AE; Surana, P; Kottur, J; Jair, DT; Basilico, F; Cecatiello, V; Pasqualato, S; Boland, A; Weichenrieder, O; Wang, B-C; Steinmetz, MO; Caffrey, M; Wang, M

doi:10.1038/nmeth.3211

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Fast native-SAD phasing for routine macromolecular structure determination

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Boland, A
Structural Biology of Selfish RNA, Max Planck Institute for Developmental Biology, Max Planck Society;
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Weichenrieder, O
Structural Biology of Selfish RNA, Max Planck Institute for Developmental Biology, Max Planck Society;
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Weinert, T., Olieric, V., Waltersperger, S., Panepucci, E., Chen, L., Zhang, H., et al. (2015). Fast native-SAD phasing for routine macromolecular structure determination. Nature Methods, 12(2), 131-133. doi:10.1038/nmeth.3211.

Cite as: https://hdl.handle.net/21.11116/0000-000A-A4F0-D

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.