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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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