Volume 54, Issue 6-2 pp. 1414-1415

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

First published: 27 September 2007
Citations: 1

Abstract

Prolyl oligopeptidase from pig muscle has been crystallized in complex with an inhibitor, using PEG 8000 and calcium acetate as precipitants. The crystals are orthorombic and the space group is P212121 with cell dimensions a = 111.8, b = 101.8, c = 72.4 Å. The asymmetric unit contains a single chain of prolyl oligopeptidase, corresponding to a specific volume of 2.55 Å3 Da−1 and a solvent content of 52%. The observed diffraction pattern extends to 2.3 Å resolution and the native crystals are well suited for structural analysis by X-ray diffraction methods.

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