Expression, purification, crystallization, data collection and preliminary biochemical characterization of methicillin-resistantStaphylococcus aureusSar2028, an aspartate/tyrosine/phenylalanine pyridoxal-5′-phosphate-dependent aminotransferase
- 28 April 2007
- journal article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Vol. 63 (5) , 452-456
- https://doi.org/10.1107/s1744309107019562
Abstract
Sar2028, an aspartate/tyrosine/phenylalanine pyridoxal-5'-phosphate-dependent aminotransferase with a molecular weight of 48,168 Da, was overexpressed in methicillin-resistant Staphylococcus aureus compared with a methicillin-sensitive strain. The protein was expressed in Escherichia coli, purified and crystallized. The protein crystallized in a primitive orthorhombic Laue group with unit-cell parameters a = 83.6, b = 91.3, c = 106.0 A, alpha = beta = gamma = 90 degrees. Analysis of the systematic absences along the three principal axes indicated the space group to be P2(1)2(1)2(1). A complete data set was collected to 2.5 A resolution.Keywords
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