4TKR
Native-SAD phasing for ThiT from Listeria monocytogenes serovar.
Summary for 4TKR
| Entry DOI | 10.2210/pdb4tkr/pdb |
| Descriptor | Thiamine transporter thia, THIAMINE DIPHOSPHATE, 2-O-octyl-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | membrane protein, transporter, native-sad phasing, multiple crystals, low energy, structural genomics, psi-biology, new york consortium on membrane protein structure, nycomps |
| Biological source | Listeria monocytogenes |
| Total number of polymer chains | 2 |
| Total formula weight | 53394.85 |
| Authors | Guo, Y.,Liu, Q.,Hendrickson, W.A.,New York Consortium on Membrane Protein Structure (NYCOMPS) (deposition date: 2014-05-27, release date: 2014-06-18, Last modification date: 2023-12-27) |
| Primary citation | Liu, Q.,Guo, Y.,Chang, Y.,Cai, Z.,Assur, Z.,Mancia, F.,Greene, M.I.,Hendrickson, W.A. Multi-crystal native SAD analysis at 6 keV. Acta Crystallogr.,Sect.D, 70:2544-2557, 2014 Cited by PubMed Abstract: Anomalous diffraction signals from typical native macromolecules are very weak, frustrating their use in de novo structure determination. Here, native SAD procedures are described to enhance signal to noise in anomalous diffraction by using multiple crystals in combination with synchrotron X-rays at 6 keV. Increased anomalous signals were obtained at 6 keV compared with 7 keV X-ray energy, which was used for previous native SAD analyses. A feasibility test of multi-crystal-based native SAD phasing was performed at 3.2 Å resolution for a known tyrosine protein kinase domain, and real-life applications were made to two novel membrane proteins at about 3.0 Å resolution. The three applications collectively serve to validate the robust feasibility of native SAD phasing at lower energy. PubMed: 25286840DOI: 10.1107/S1399004714013376 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.0023 Å) |
Structure validation
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