Abstract
Single crystals of the RuvC protein, an Escherichia coli endonuclease specific for Holliday junctions, were grown by the microdialysis method. The crystals belong to the space group P2(1), with unit cell dimensions a = 72.8 A, b = 139.6 A, c = 32.4 A and beta = 93.0 degrees, and contain four molecules in an asymmetric unit. Diffraction data to a Bragg spacing of 2.5 A resolution has been obtained using a synchrotron X-ray source.
MeSH terms
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / isolation & purification
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Crystallization
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Crystallography, X-Ray
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DNA Repair / genetics
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Endodeoxyribonucleases / chemistry*
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Endodeoxyribonucleases / genetics
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Endodeoxyribonucleases / isolation & purification
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Escherichia coli / metabolism*
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Escherichia coli Proteins*
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Recombination, Genetic
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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ruvC protein, E coli
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Endodeoxyribonucleases