Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase fromStaphylococcus aureus
- 23 May 2008
- journal article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Vol. 64 (6), 520-523
- https://doi.org/10.1107/s1744309108012244
Abstract
Biotin protein ligase from Staphylococcus aureus catalyses the biotinylation of acetyl-CoA carboxylase and pyruvate carboxylase. Recombinant biotin protein ligase from S. aureus has been cloned, expressed and purified. Crystals were grown using the hanging-drop vapour-diffusion method using PEG 8000 as the precipitant at 295 K. X-ray diffraction data were collected to 2.3 A resolution from crystals using synchrotron X-ray radiation at 100 K. The diffraction was consistent with the tetragonal space group P4(2)2(1)2, with unit-cell parameters a = b = 93.665, c = 131.95.Keywords
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