Purification, crystallization and data collection of methicillin-resistant Staphylococcus aureus Sar2676, a pantothenate synthetase

Jaldappagari Seetharamappa, Muse Oke, Huanting Liu, Stephen A. McMahon, Kenneth A. Johnson, Lester Carter, Mark Dorward, Michal Zawadzki, Ian M. Overton, C. A.Johannes Van Niekirk, Shirley Graham, Catherine H. Botting, Garry L. Taylor, Malcolm F. White, Geoffrey J. Barton, Peter J. Coote, James H. Naismith

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

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 languageEnglish
Pages (from-to)488-491
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number6
DOIs
Publication statusPublished - 5 May 2007

Keywords

  • Methicillin-resistant Staphylococcus aureus
  • Pantothenate synthetase
  • Sar2676

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