Open AccessPurification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus
Author(s) -
Pendini Nicole R.,
Polyak Steve W.,
Booker Grant W.,
Wallace John C.,
Wilce Matthew C. J.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108012244
Subject(s) - biotin , pyruvate carboxylase , dna ligase , tetragonal crystal system , crystallization , staphylococcus aureus , crystallography , chemistry , biochemistry , biology , crystal structure , enzyme , bacteria , organic chemistry , genetics
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 Å resolution from crystals using synchrotron X‐ray radiation at 100 K. The diffraction was consistent with the tetragonal space group P 4 2 2 1 2, with unit‐cell parameters a = b = 93.665, c = 131.95.