Crystallization and preliminary X-ray analysis of porcine muscle prolyl oligopeptidase

Prolyl oligopeptidase from pig muscle has been crystallized in complex with an inhibitor, using PEG 8000 and calcium acetate as precipitants. The crys tals are orthorombic and the space group is P2(1)2(1)2(1) With cell dimensi ons a = 111.8, b = 101.8, c = 72.4 Angstrom. The asymmetric unit contains a single chain of prolyl oligopeptidase,corresponding to a specific volume o f 2.55 Angstrom(3) Da(-1) and solvent-content of 52%. The observed diffract ion pattern extends to 2.3 Angstrom resolution and the native crystals are well suited for structural analysis by X-ray diffraction methods.