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

Authors :
Seetharamappa J
Oke M
Liu H
McMahon SA
Johnson KA
Carter L
Dorward M
Zawadzki M
Overton IM
van Niekirk CA
Graham S
Botting CH
Taylor GL
White MF
Barton GJ
Coote PJ
Naismith JH
Source :
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2007 May 01; Vol. 63 (Pt 5), pp. 452-6. Date of Electronic Publication: 2007 Apr 28.
Publication Year :
2007

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.

Details

Language :
English
ISSN :
1744-3091
Volume :
63
Issue :
Pt 5
Database :
MEDLINE
Journal :
Acta crystallographica. Section F, Structural biology and crystallization communications
Publication Type :
Academic Journal
Accession number :
17565195
Full Text :
https://doi.org/10.1107/S1744309107019562