Abstract
Recombinant amylosucrase from Neisseria polysaccharea was crystallized by the vapour-diffusion procedure in the presence of polyethylene glycol 6000. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 95.7, b = 117.2, c = 62.1 A, and diffract to 1.6 A resolution. A p-chloromercuribenzene sulfonate (pcmbs) derivative has been identified and a selenomethionine-substituted protein has been produced and crystallized.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / biosynthesis
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Bacterial Proteins / chemistry
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Bacterial Proteins / isolation & purification
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Circular Dichroism
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Crystallization
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Crystallography, X-Ray
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Escherichia coli / chemistry
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Escherichia coli / enzymology
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Glucosyltransferases / biosynthesis
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Glucosyltransferases / chemistry*
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Glucosyltransferases / isolation & purification
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Neisseria / enzymology*
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry*
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Recombinant Proteins / isolation & purification
Substances
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Bacterial Proteins
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Recombinant Proteins
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Glucosyltransferases
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amylosucrase