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 Å, α = 87.2, β = 81.2, γ = 68.4°. A complete data set has been collected to 2.3 Å 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 - 5 May 2007 |
Keywords
- Methicillin-resistant Staphylococcus aureus
- Pantothenate synthetase
- Sar2676
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics
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