Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/51853
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Type: Journal article
Title: Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus
Author: Pendini, N.
Polyak, S.
Booker, G.
Wallace, J.
Wilce, M.
Citation: Acta Crystallographica Section F: Structural Biology and Crystallization Communications Online, 2008; 64 Part 6(6):520-523
Publisher: Blackwell Munksgaard
Issue Date: 2008
ISSN: 1744-3091
1744-3091
Statement of
Responsibility: 
N. R. Pendini, S. W. Polyak, G. W. Booker, J. C. Wallace and M. C. J. Wilce
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 P4₂2₁2, with unit-cell parameters a = b = 93.665, c = 131.95.
Keywords: biotin protein ligase
Staphylococcus aureus.
DOI: 10.1107/S1744309108012244
Published version: http://dx.doi.org/10.1107/s1744309108012244
Appears in Collections:Aurora harvest
Molecular and Biomedical Science publications

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