Abstract
The gene SA239 from Staphylococcus aureus encodes a ribokinase that catalyzes the phosphorylation of D-ribose to produce ribose-5-phosphate. Sa239 was crystallized using the hanging-drop vapour-diffusion method. The crystals diffracted to 2.9 A resolution and belonged to space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 91.8, c = 160.7 A. Preliminary crystallographic analysis revealed that the Matthews coefficient V(M) was 3.01 A(3) Da(-1), indicating the presence of one molecule in the asymmetric unit.
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 / genetics
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Bacterial Proteins / isolation & purification*
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Bacterial Proteins / metabolism
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Binding Sites
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Cloning, Molecular
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Crystallization
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Crystallography, X-Ray
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Data Collection
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Escherichia coli / genetics
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Genes, Bacterial
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Phosphotransferases (Alcohol Group Acceptor) / chemistry*
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Phosphotransferases (Alcohol Group Acceptor) / genetics
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Phosphotransferases (Alcohol Group Acceptor) / isolation & purification*
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Phosphotransferases (Alcohol Group Acceptor) / metabolism
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Protein Binding
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / isolation & purification
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Recombinant Fusion Proteins / metabolism
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Staphylococcus aureus / enzymology*
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Statistics as Topic
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X-Ray Diffraction
Substances
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Bacterial Proteins
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Recombinant Fusion Proteins
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Phosphotransferases (Alcohol Group Acceptor)
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ribokinase