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

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 A, alpha = 87.2, beta = 81.2, gamma = 68.4 degrees . A complete data set has been collected to 2.3 A 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)488-91
Number of pages4
JournalActa Crystallographica Section F Structural Biology and Crystallization Communications
Volume63
Issue numberPt 6
DOIs
Publication statusPublished - 1 Jun 2007

Keywords

  • Bacterial Proteins
  • Crystallization
  • Crystallography, X-Ray
  • Methicillin Resistance
  • Peptide Synthases
  • Staphylococcus aureus

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