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CRYSTALLOGRAPHY OF BIOLOGICAL MACROMOLECULES
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2005
Year
Unknown Venue
BiochemistryBs139 CrystalNatural SciencesProtein X-ray CrystallographyDna ReplicationMolecular BiologyStructural GenomicsPurine BiosynthesisCrystallographyStructural Biology
C257 obtained and 6 structures were determined. Among them, Bs139 protein functions as phosphoribosylglycinamide formyltransferase (GART), an important enzyme in the de novo pathway of purine biosynthesis. Bs139 crystal diffracted to 2.5 A resolution at home Xray source and the structure was determined by molecular replacement (MR). Bs154 protein is a putative deoxyuridine 5'-triphosphate nucleotidehydrolase (dUTPase), which plays important role in DNA replication. Se-YosS crystal diffraction datasets were collected at Beijing Synchrotron Radiation Facility (BSRF) and the structure was determined by multi-wavelength anomalous diffraction (MAD) method.