Abstract
The terminal oxygenase component of the biphenyl dioxygenase (BphA1A2 complex) was over-expressed with a novel over expression system in recombinant Rhodococcus strain and purified. The purified enzyme has been crystallized by the hanging drop vapor diffusion method and subjected to X-ray diffraction analysis. The crystals belong to the tetragonal system in the space group P4(1)2(1)2 or P4(3)2(1)2 and diffract to better than 2.2A resolution.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cloning, Molecular
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Crystallization
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Crystallography, X-Ray
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Data Interpretation, Statistical
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Gene Expression Regulation, Enzymologic
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Iron-Sulfur Proteins / chemistry*
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Iron-Sulfur Proteins / genetics
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Iron-Sulfur Proteins / isolation & purification
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Oxygenases / chemistry*
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Oxygenases / genetics
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Oxygenases / isolation & purification
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Rhodococcus / enzymology*
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Rhodococcus / genetics
Substances
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Iron-Sulfur Proteins
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Recombinant Proteins
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Oxygenases
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biphenyl-2,3-dioxygenase