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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.

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.

SUBMITTER: Seetharamappa J 

PROVIDER: S-EPMC2335000 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature

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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.

Seetharamappa Jaldappagari J   Oke Muse M   Liu Huanting H   McMahon Stephen A SA   Johnson Kenneth A KA   Carter Lester L   Dorward Mark M   Zawadzki Michal M   Overton Ian M IM   van Niekirk C A Johannes CA   Graham Shirley S   Botting Catherine H CH   Taylor Garry L GL   White Malcolm F MF   Barton Geoffrey J GJ   Coote Peter J PJ   Naismith James H JH  

Acta crystallographica. Section F, Structural biology and crystallization communications 20070428 Pt 5

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 systemat  ...[more]

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