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https://hdl.handle.net/2440/51853
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DC Field | Value | Language |
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dc.contributor.author | Pendini, N. | - |
dc.contributor.author | Polyak, S. | - |
dc.contributor.author | Booker, G. | - |
dc.contributor.author | Wallace, J. | - |
dc.contributor.author | Wilce, M. | - |
dc.date.issued | 2008 | - |
dc.identifier.citation | Acta Crystallographica Section F: Structural Biology and Crystallization Communications Online, 2008; 64 Part 6(6):520-523 | - |
dc.identifier.issn | 1744-3091 | - |
dc.identifier.issn | 1744-3091 | - |
dc.identifier.uri | http://hdl.handle.net/2440/51853 | - |
dc.description.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. | - |
dc.description.statementofresponsibility | N. R. Pendini, S. W. Polyak, G. W. Booker, J. C. Wallace and M. C. J. Wilce | - |
dc.language.iso | en | - |
dc.publisher | Blackwell Munksgaard | - |
dc.source.uri | http://dx.doi.org/10.1107/s1744309108012244 | - |
dc.subject | biotin protein ligase | - |
dc.subject | Staphylococcus aureus. | - |
dc.title | Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1107/S1744309108012244 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Polyak, S. [0000-0002-8458-5194] | - |
dc.identifier.orcid | Booker, G. [0000-0001-7207-4699] | - |
Appears in Collections: | Aurora harvest Molecular and Biomedical Science publications |
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