Abstract
The type II restriction endonuclease BamHI has been expressed in E. coli, producing 100-fold more enzyme than the wild type Bacillus amyloliquefaciens H strain. This high yield has facilitated purification to homogeneity of large amounts of the enzyme, along with its crystallization in a form which diffracts to at least 1.9 A in X-ray analysis.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacillus / enzymology
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Cloning, Molecular
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Crystallization
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Deoxyribonuclease BamHI / biosynthesis*
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Deoxyribonuclease BamHI / chemistry
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Deoxyribonuclease BamHI / isolation & purification
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / genetics*
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Plasmids
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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X-Ray Diffraction
Substances
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Recombinant Proteins
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Deoxyribonuclease BamHI