Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/51853
Citations
Scopus Web of Science® Altmetric
?
?
Full metadata record
DC FieldValueLanguage
dc.contributor.authorPendini, N.-
dc.contributor.authorPolyak, S.-
dc.contributor.authorBooker, G.-
dc.contributor.authorWallace, J.-
dc.contributor.authorWilce, M.-
dc.date.issued2008-
dc.identifier.citationActa Crystallographica Section F: Structural Biology and Crystallization Communications Online, 2008; 64 Part 6(6):520-523-
dc.identifier.issn1744-3091-
dc.identifier.issn1744-3091-
dc.identifier.urihttp://hdl.handle.net/2440/51853-
dc.description.abstractBiotin 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.statementofresponsibilityN. R. Pendini, S. W. Polyak, G. W. Booker, J. C. Wallace and M. C. J. Wilce-
dc.language.isoen-
dc.publisherBlackwell Munksgaard-
dc.source.urihttp://dx.doi.org/10.1107/s1744309108012244-
dc.subjectbiotin protein ligase-
dc.subjectStaphylococcus aureus.-
dc.titlePurification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus-
dc.typeJournal article-
dc.identifier.doi10.1107/S1744309108012244-
pubs.publication-statusPublished-
dc.identifier.orcidPolyak, S. [0000-0002-8458-5194]-
dc.identifier.orcidBooker, G. [0000-0001-7207-4699]-
Appears in Collections:Aurora harvest
Molecular and Biomedical Science publications

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.