CRYSTALLOGRAPHIC DATA FOR THE DD-CARBOXYPEPTIDASE-ENDOPEPTIDASE OF LOW PENICILLIN SENSITIVITY EXCRETED BY STREPTOMYCES-ALBUS G

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 a = 51.1 A ̊, b = 49.7 A ̊, c = 38.7 A ̊, β = 100.6 ° 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% ( w v) polyethylene glycol exhibits enzyme activity on the substrate Ac2-l-Lys-d-Ala-d-Ala. © 1979.