Fast native-SAD phasing for routine macromolecular structure determination.
| Title | Fast native-SAD phasing for routine macromolecular structure determination. |
| Publication Type | Journal Article |
| Year of Publication | 2015 |
| Authors | 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, Nair DT, Basilico F, Cecatiello V, Pasqualato S, Boland A, Weichenrieder O, Wang B-C, Steinmetz MO, Caffrey M, Wang M |
| Journal | Nat Methods |
| Volume | 12 |
| Issue | 2 |
| Pagination | 131-3 |
| Date Published | 2015 Feb |
| ISSN | 1548-7105 |
| Keywords | Animals, DNA-Binding Proteins, Humans, Membrane Proteins, Models, Molecular, Multiprotein Complexes, Protein Conformation, Software, Synchrotrons, X-Ray Diffraction |
| 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. |
| DOI | 10.1038/nmeth.3211 |
| Alternate Journal | Nat. Methods |
| PubMed ID | 25506719 |