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Protein Pept Lett ; 10(4): 412-7, 2003 Aug.
Article in English | MEDLINE | ID: mdl-14529495

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.


Subject(s)
Iron-Sulfur Proteins/chemistry , Oxygenases/chemistry , Rhodococcus/enzymology , Cloning, Molecular , Crystallization , Crystallography, X-Ray , Data Interpretation, Statistical , Gene Expression Regulation, Enzymologic , Iron-Sulfur Proteins/genetics , Iron-Sulfur Proteins/isolation & purification , Oxygenases/genetics , Oxygenases/isolation & purification , Recombinant Proteins/chemistry , Recombinant Proteins/isolation & purification , Rhodococcus/genetics
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