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Crystallization Of The Terminal Oxygenase Component Of Biphenyl Dioxygenase Derived From Rhodococcus Sp. Strain Rha1

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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 2.2Å resolution.

Keywords: biphenyl dioxygenase; non-heme iron; polychlorinated biphenyl; rieske iron-sulfur center

Document Type: Review Article


Affiliations: Division of Protein Engineering and Division of Microbial Engineering, Department of BioEngineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan

Publication date: August 1, 2003

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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