Crystallographic data for a penicillin receptor : exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61.期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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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

Institution:	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 (M_r = 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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