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

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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 Å, α = β = γ = 90°. Analysis of the systematic absences along the three principal axes indicated the space group to be P212 121. A complete data set was collected to 2.5 Å resolution. © International Union of Crystallography 2007.

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Seetharamappa, J., Oke, M., Liu, H., McMahon, S. A., Johnson, K. A., Carter, L., … Naismith, J. H. (2007). Expression, purification, crystallization, data collection and preliminary biochemical characterization of methicillin-resistant Staphylococcus aureus Sar2028, an aspartate/tyrosine/phenylalanine pyridoxal-5′-phosphate- dependent aminotransferase. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(5), 452–456. https://doi.org/10.1107/S1744309107019562

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