Expression, purification, crystallization, data collection and preliminary biochemical characterization of methicillin-resistant Staphylococcus aureus Sar2028, an aspartate/tyrosine/phenylalanine pyridoxal-5′-phosphate-dependent aminotransferase
- Scottish Structural Facility and Centre for Biomolecular Sciences, The University, St Andrews KY16 9ST,Scotland (United Kingdom)
- Scottish Structural Facility and School of Life Sciences Research, University of Dundee, Dow Street, Dundee DD1 5EH,Scotland (United Kingdom)
As part of work on S. aureus, the crystallization of Sar2028, a protein that is upregulated in MRSA, is reported. 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 Å, α = β = γ = 90°. Analysis of the systematic absences along the three principal axes indicated the space group to be P2{sub 1}2{sub 1}2{sub 1}. A complete data set was collected to 2.5 Å resolution.
- OSTI ID:
- 22360324
- Journal Information:
- Acta Crystallographica. Section F, Vol. 63, Issue Pt 5; Other Information: PMCID: PMC2335000; PMID: 17565195; PUBLISHER-ID: en5236; OAI: oai:pubmedcentral.nih.gov:2335000; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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