@article {897, title = {Fast native-SAD phasing for routine macromolecular structure determination.}, journal = {Nat Methods}, volume = {12}, year = {2015}, month = {2015 Feb}, pages = {131-3}, 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.

}, keywords = {Animals, DNA-Binding Proteins, Humans, Membrane Proteins, Models, Molecular, Multiprotein Complexes, Protein Conformation, Software, Synchrotrons, X-Ray Diffraction}, issn = {1548-7105}, doi = {10.1038/nmeth.3211}, author = {Weinert, Tobias and Olieric, Vincent and Waltersperger, Sandro and Panepucci, Ezequiel and Chen, Lirong and Zhang, Hua and Zhou, Dayong and Rose, John and Ebihara, Akio and Kuramitsu, Seiki and Li, Dianfan and Howe, Nicole and Schnapp, Gisela and Pautsch, Alexander and Bargsten, Katja and Prota, Andrea E and Surana, Parag and Kottur, Jithesh and Nair, Deepak T and Basilico, Federica and Cecatiello, Valentina and Pasqualato, Sebastiano and Boland, Andreas and Weichenrieder, Oliver and Wang, Bi-Cheng and Steinmetz, Michel O and Caffrey, Martin and Wang, Meitian} }