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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry
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Bacterial Proteins / isolation & purification*
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Biotin / chemistry*
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Biotin / genetics
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Biotinylation
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Carbon-Nitrogen Ligases / chemistry*
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Carbon-Nitrogen Ligases / genetics
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Carbon-Nitrogen Ligases / isolation & purification*
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Cloning, Molecular
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Crystallization
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Crystallography, X-Ray
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Escherichia coli / genetics
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Histidine / chemistry
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Molecular Weight
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Staphylococcus aureus / enzymology*
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X-Ray Diffraction
Substances
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Bacterial Proteins
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Recombinant Proteins
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Histidine
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Biotin
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Carbon-Nitrogen Ligases