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 angstrom, 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 angstrom resolution.
| Original language | English |
|---|---|
| Pages (from-to) | 452-456 |
| Number of pages | 5 |
| Journal | Acta Crystallographica. Section F, Structural biology and crystallization communications |
| Volume | 63 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - May 2007 |
Keywords
- PROTEINS
- MRSA
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Dive into the research topics of 'Expression, purification, crystallization, data collection and preliminary biochemical characterization of methicillin-resistant Staphylococcus aureus Sar2028, an aspartate/tyrosine/phenylalanine pyridoxal-5'-phosphate-dependent aminotransferase..'. Together they form a unique fingerprint.Projects
- 1 Finished
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BBSRC BBS/B/14426: SPORT
Naismith, J. (PI)
Biotechnology and Biological Sciences Research Council
18/10/04 → 30/04/12
Project: Standard
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