Open AccessExpression, purification, crystallization, data collection and preliminary biochemical characterization of methicillin‐resistant Staphylococcus aureus Sar2028, an aspartate/tyrosine/phenylalanine pyridoxal‐5′‐phosphate‐dependent aminotransferase
Author(s) -
Seetharamappa Jaldappagari,
Oke Muse,
Liu Huanting,
McMahon Stephen A.,
Carter Lester,
Graham Shirley,
Dorward Mark,
Johnson Kenneth A.,
Zawadzki Michal,
Overton Ian M.,
White Malcolm F.,
Botting Catherine H.,
Taylor Garry L.,
Coote Peter J.,
Barton Geoffrey J.,
Van Niekirk C. A. Johannes,
Naismith James H.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107019562
Subject(s) - phenylalanine , pyridoxal phosphate , staphylococcus aureus , crystallization , tyrosine , biochemistry , chemistry , pyridoxal , microbiology and biotechnology , phosphate , enzyme , biology , bacteria , amino acid , cofactor , organic chemistry , genetics
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 Å, α = β = γ = 90°. Analysis of the systematic absences along the three principal axes indicated the space group to be P 2 1 2 1 2 1 . A complete data set was collected to 2.5 Å resolution.