期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 70, 期 -, 页码 1249-1251出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X14016458
关键词
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资金
- European Molecular Biology Laboratory [MX-40]
- Autonomous Province of Bolzano (project: A Structural Genomics Approach for the Study of the Virulence and Pathogenesis of E. amylovora)
- Free University of Bolzano (project GAMEs: Galactose and Glucuronic Acid Metabolism in Erwinia spp.)
Glucose-1-phosphate uridylyltransferase from Erwinia amylovora CFPB1430 was expressed as a His-tag fusion protein in Escherichia coli. After tag removal, the purified protein was crystallized from 100 mM Tris pH 8.5, 2 M ammonium sulfate, 5% ethylene glycol. Diffraction data sets were collected to a maximum resolution of 2.46 angstrom using synchrotron radiation. The crystals belonged to the hexagonal space group P6(2), with unit-cell parameters a = 80.67, b = 80.67, c = 169.18. The structure was solved by molecular replacement using the structure of the E. coli enzyme as a search model.
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