4TKS
Native-SAD phasing for human EGFR kinase domain.
Summary for 4TKS
Entry DOI | 10.2210/pdb4tks/pdb |
Descriptor | Epidermal growth factor receptor (1 entity in total) |
Functional Keywords | egfr kinase domain, native-sad phasing, multiple crystals, low energy, transferase |
Biological source | Homo sapiens (Human) |
Cellular location | Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted: P00533 |
Total number of polymer chains | 1 |
Total formula weight | 37707.58 |
Authors | Cai, Z.,Greene, M.I.,Liu, Q. (deposition date: 2014-05-27, release date: 2014-10-08, 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 (3.2017 Å) |
Structure validation
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