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4TKS

Native-SAD phasing for human EGFR kinase domain.

Summary for 4TKS
Entry DOI10.2210/pdb4tks/pdb
DescriptorEpidermal growth factor receptor (1 entity in total)
Functional Keywordsegfr kinase domain, native-sad phasing, multiple crystals, low energy, transferase
Biological sourceHomo sapiens (Human)
Cellular locationCell membrane; Single-pass type I membrane protein. Isoform 2: Secreted: P00533
Total number of polymer chains1
Total formula weight37707.58
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 citationLiu, 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: 25286840
DOI: 10.1107/S1399004714013376
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2017 Å)
Structure validation

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