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

J Seetharamappa, Muse Oke, Huanting Liu, Stephen McMahon, Kenneth Alan Johnson, Lester Carter, M Dorward, M Zawadzki, IM Overton, CA van Niekirk, S Graham, Catherine Helen Botting, Garry Lindsay Taylor, Malcolm Frederick White, GJ Barton, Peter John Coote, James Henderson 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 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 languageEnglish
Pages (from-to)488-491
Number of pages4
JournalActa Crystallographica. Section F, Structural biology and crystallization communications
Volume63
Issue number6
DOIs
Publication statusPublished - Jun 2007

Keywords

  • MYCOBACTERIUM-TUBERCULOSIS
  • CRYSTAL-STRUCTURE
  • ESCHERICHIA-COLI
  • BIOSYNTHESIS
  • SURVEILLANCE
  • BACTEREMIA

Fingerprint

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.
  • BBSRC BBS/B/14426: SPORT

    Naismith, J. (PI)

    BBSRC

    18/10/0430/04/12

    Project: Standard

Cite this