Crystallographic data for the DD-carboxypeptidase-endopeptidase of low penicillin sensitivity excreted by Streptomyces albus g. |
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Authors: | O Dideberg J M Frère J M Ghuysen |
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Affiliation: | Laboratoire de Cristallographie Institut de Physique B5 Université de Liège au Sart Tilman B-4000 Liège, Belgique;Service de Microbiologie, Faculté de Médecine Université de Liège au Sart Tilman Institut de Botanique B22 B-4000 Liège, Belgique |
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Abstract: | The dd-carboxypeptidase-endopeptidase of low penicillin sensitivity that is excreted by Streptomyces albus G has been crystallized from a polyethylene glycol (Mr 6000 to 7500) solution at pH 8.0. X-ray examination of the prismatic crystals shows that the space group is P21 with unit cell dimensions and one molecule in the asymmetric unit. A crystal suspension made in 50 mm-Tris · HCl buffer (pH 8.0) supplemented with 5 mm-MgCl2 and 16% () polyethylene glycol exhibits enzyme activity on the substrate Ac2-l-Lys-d-Ala-d-Ala. |
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