Open AccessPurification, crystallization and data collection of methicillin‐resistant Staphylococcus aureus Sar2676, a pantothenate synthetase
Author(s) -
Seetharamappa Jaldappagari,
Oke Muse,
Liu Huanting,
McMahon Stephen A.,
Johnson Kenneth A.,
Carter Lester,
Dorward Mark,
Zawadzki Michal,
Overton Ian M.,
Van Niekirk C. A. Johannes,
Graham Shirley,
Botting Catherine H.,
Taylor Garry L.,
White Malcolm F.,
Barton Geoffrey J.,
Coote Peter J.,
Naismith James H.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107020362
Subject(s) - triclinic crystal system , staphylococcus aureus , crystallization , monomer , molecular replacement , protein data bank (rcsb pdb) , escherichia coli , methicillin resistant staphylococcus aureus , crystallography , chemistry , microbiology and biotechnology , biology , crystal structure , stereochemistry , biochemistry , bacteria , genetics , organic chemistry , gene , polymer
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.