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

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 A, 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 A resolution.

Cite this paper

@article{Seetharamappa2007ExpressionPC, title={Expression, purification, crystallization, data collection and preliminary biochemical characterization of methicillin-resistant Staphylococcus aureus Sar2028, an aspartate/tyrosine/phenylalanine pyridoxal-5'-phosphate-dependent aminotransferase.}, author={Jaldappagari Seetharamappa and Muse Oke and Huanting Liu and Stephen A. McMahon and K A Johnson and Lester G. Carter and Mark Dorward and Michal Zawadzki and Ian M. Overton and C A Johannes van Niekirk and Shirley Graham and Catherine H. Botting and Garry L. Taylor and Malcolm F. White and Geoffrey J. Barton and Peter J. Coote and James H. Naismith}, journal={Acta crystallographica. Section F, Structural biology and crystallization communications}, year={2007}, volume={63 Pt 5}, pages={452-6} }