Abstract
Sar2676, a pantothenate synthetase with a molecular weight of 31 419 Da from methicillin- resistant Staphylococcus aureus, has been expressed, purified and crystallized at 293 K. The protein crystallizes in a primitive triclinic lattice, with unit-cell parameters a = 45.3, b = 60.5, c = 117.6 angstrom, alpha = 87.2, beta = 81.2, gamma = 68.4 degrees. A complete data set has been collected to 2.3 angstrom resolution at the ESRF. Consideration of the likely solvent content suggested the asymmetric unit to contain four molecules. This has been confirmed by molecular- replacement phasing calculations, which give a solution with four monomers using a monomer of pantothenate synthetase from Escherichia coli ( PDB code 1iho), which is 41% identical to Sar2676, as a search model.
| Original language | English |
|---|---|
| Pages (from-to) | 488-491 |
| Number of pages | 4 |
| Journal | Acta Crystallographica. Section F, Structural biology and crystallization communications |
| Volume | 63 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - Jun 2007 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Keywords
- MYCOBACTERIUM-TUBERCULOSIS
- CRYSTAL-STRUCTURE
- ESCHERICHIA-COLI
- BIOSYNTHESIS
- SURVEILLANCE
- BACTEREMIA
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Dive into the research topics of 'Purification, crystallization and data collection of methicillin-resistant Staphylococcus aureus Sar2676, a pantothenate synthetase.'. 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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