Abstract
The water-soluble portion of rat heme oxygenase-1 which lacks 22 hydrophobic amino-acid residues at the C-terminus was expressed in E. coli and crystallized in the form of a complex with heme by the vapor-diffusion method using polyethylene glycol 4000 as the precipitant. The crystals belong to the tetragonal space group P41212 or P43212, with unit-cell dimensions of a = b = 56.7, c = 186. 7 A. The crystal contains one heme-heme oxygenase-1 complex in an asymmetric unit and diffracts X-rays beyond 3.0 A resolution with a conventional X-ray source.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Binding Sites
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Crystallization
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Crystallography, X-Ray
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Heme / chemistry*
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Heme / metabolism
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Heme Oxygenase (Decyclizing) / chemistry*
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Heme Oxygenase (Decyclizing) / isolation & purification
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Heme Oxygenase (Decyclizing) / metabolism
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Heme Oxygenase-1
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Macromolecular Substances
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Protein Binding
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Protein Conformation*
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Rats
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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
Substances
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Macromolecular Substances
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Recombinant Fusion Proteins
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Heme
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Heme Oxygenase (Decyclizing)
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Heme Oxygenase-1