Expression, purification, crystallization, data collection and preliminary biochemical characterization of methicillin-resistant Staphylococcus aureus Sar2028, an aspartate/tyrosine/phenylalanine pyridoxal-5'-phosphate-dependent aminotransferase..

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

4 Citations (Scopus)

Abstract

Sar2028, an aspartate/tyrosine/phenylalanine pyridoxal-5'-phosphate-dependent aminotransferase with a molecular weight of 48 168 Da, was overexpressed in methicillin-resistant Staphylococcus aureus compared with a methicillin-sensitive strain. The protein was expressed in Escherichia coli, purified and crystallized. The protein crystallized in a primitive orthorhombic Laue group with unit-cell parameters a = 83.6, b = 91.3, c = 106.0 angstrom, alpha = beta = gamma = 90 degrees. Analysis of the systematic absences along the three principal axes indicated the space group to be P2(1)2(1)2(1). A complete data set was collected to 2.5 angstrom resolution.

Original languageEnglish
Pages (from-to)452-456
Number of pages5
JournalActa Crystallographica. Section F, Structural biology and crystallization communications
Volume63
Issue number5
DOIs
Publication statusPublished - May 2007

Keywords

  • PROTEINS
  • MRSA

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  • BBSRC BBS/B/14426: SPORT

    Naismith, J.

    BBSRC

    18/10/0430/04/12

    Project: Standard

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