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  • Title: Crystallization and preliminary X-ray crystallographic analysis of the protease inhibitor ecotin in complex with chymotrypsin.
    Author: Lee CS, Seong IS, Song HK, Chung CH, Suh SW.
    Journal: Acta Crystallogr D Biol Crystallogr; 1999 May; 55(Pt 5):1091-2. PubMed ID: 10216315.
    Abstract:
    Ecotin, a homodimeric protein composed of 142-residue subunits, is a novel protease inhibitor present in the periplasm of Escherichia coli. It shows a broad inhibitory specificity towards a group of serine proteases and binds two molecules of protease to form a tetrameric complex in a distinct chelation mechanism. The ecotin-chymotrypsin complex has been crystallized in the triclinic space group P1 with unit-cell parameters a = 57.29, b = 57.39, c = 79.75 A, alpha = 91.49, beta = 88.63 and gamma = 112.45 degrees. The asymmetric unit contains the whole tetrameric complex, consisting of two molecules of chymotrypsin bound to the ecotin dimer, with a corresponding crystal volume per protein mass (VM) of 2.58 A3 Da-1 and a solvent fraction of 48.9%. The crystals diffract beyond 2.0 A with Cu Kalpha X-rays and are very stable in the X-ray beam. Native X-ray data have been collected from a crystal to approximately 2.0 A Bragg spacing.
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