Abstract
Crystals of the penicillin binding protein 4 (PBP4) from Escherichia coli have been obtained at 37 degrees C from liquid to liquid diffusion experiments in capillaries. PBP4 was dissolved in a 1.0 M ammonium sulphate solution, buffered at pH 7.2, to a concentration of 5 mg/ml, and was layered on top of a 1.6 to 2.2 M ammonium sulphate solution. Crystals appeared within four to six weeks. They belong to space group C222 with cell dimensions a = 68.5 A, b = 100.5 A and c = 137.0 A, and diffract to at least 2.8 A resolution. There is one molecule with a molecule mass of 49,568 Da in the asymmetric unit.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins*
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Carrier Proteins / chemistry*
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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 Proteins*
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Hexosyltransferases*
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Molecular Sequence Data
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Muramoylpentapeptide Carboxypeptidase / chemistry*
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Penicillin-Binding Proteins
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Penicillins / metabolism*
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Peptidyl Transferases*
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Sequence Homology, Amino Acid
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Serine-Type D-Ala-D-Ala Carboxypeptidase*
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beta-Lactamases / chemistry
Substances
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Bacterial Proteins
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Carrier Proteins
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Escherichia coli Proteins
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Penicillin-Binding Proteins
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Penicillins
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Peptidyl Transferases
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Hexosyltransferases
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Serine-Type D-Ala-D-Ala Carboxypeptidase
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penicillin-binding protein 4, E coli
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Muramoylpentapeptide Carboxypeptidase
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beta-Lactamases