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Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus.

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 P4(2)2(1)2, with unit-cell parameters a = b = 93.665, c = 131.95.

SUBMITTER: Pendini NR

PROVIDER: S-EPMC2496860 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus.

Pendini Nicole R NR Polyak Steve W SW Booker Grant W GW Wallace John C JC Wilce Matthew C J MC

Acta crystallographica. Section F, Structural biology and crystallization communications 20080523 Pt 6

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 spa ...[more]

PMID: 18540065

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