Abstract
The Escherichia coli ytfG gene product, with NAD(P)H:quinone oxidoreductase activity, was crystallized by the hanging-drop vapour-diffusion method at 296 K. A 1.78 A data set has been collected using synchrotron radiation at Pohang Light Source, South Korea. The crystal belongs to the primitive trigonal system, with unit-cell parameters a = b = 81.7, c = 76.8 A. Analysis of the packing density shows that the asymmetric unit probably contains one monomer, with a solvent content of 48.8%.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Crystallization
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Crystallography, X-Ray / methods*
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Cytoplasm / metabolism
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Escherichia coli / enzymology*
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Escherichia coli / metabolism
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Escherichia coli Proteins / chemistry*
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NADH, NADPH Oxidoreductases / chemistry*
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Oxidoreductases / chemistry
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Polyethylene Glycols / chemistry
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Polymerase Chain Reaction
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Recombinant Proteins / chemistry
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Solvents
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Synchrotrons
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Temperature
Substances
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Escherichia coli Proteins
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Recombinant Proteins
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Solvents
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Polyethylene Glycols
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Oxidoreductases
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NADH, NADPH Oxidoreductases
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ytfG protein, E coli