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Crystallographic data for a penicillin receptor : exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61.
Authors:J R Knox  M L DeLucia  N S Murthy  J A Kelly  P C Moews  J M Frére  J M Ghuysen
Affiliation:Biological Sciences Group and Institute of Materials Science University of Connecticut Storrs, CT 06268, U.S.A.;Service de Microbiologie Faculté de Médecine, Institut de Botanique Université de Liége, Sart Tilman, 4000 Liége, Belgium
Abstract:A pencillin-sensitive enzyme, the exocellular dd-carboxypeptidase-transpeptidase from Streptomyces R61, has been crystallized from polyethylene glycol (Mr = 6000 to 7500) solution at pH 7·6. X-ray examination of the orthorhombic crystals shows the space group is P212121, with unit cell dimensions a = 51·1 A?, b = 67·4 A?, and c = 102·9 A?. With four molecules of molecular weight 38,000, the A?3/dalton ratio for the cell is 2·33. The crystals are stable to irradiation for 75 hours and are suitable for structure analysis to at least 2·4 Å resolution. The radius of gyration of the molecule in solution at pH 6.8 is 20.8 Å.
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