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  • Title: Cloning, purification, crystallization and preliminary X-ray diffraction analysis of the antistasin-type inhibitor ghilanten (domain I) from Haementeria ghilianii in complex with porcine beta-trypsin.
    Author: Rester U, Bode W, Sampaio CA, Auerswald EA, Lopes AP.
    Journal: Acta Crystallogr D Biol Crystallogr; 2001 Jul; 57(Pt 7):1038-41. PubMed ID: 11418776.
    Abstract:
    Ghilanten, isolated from the leech Haementeria ghilianii, is a potent two-domain anticoagulant protein homologous to the factor Xa inhibitor antistasin. A synthetic gene encoding the amino-terminal domain of ghilanten (ghilanten-D1) was constructed, expressed in the methylotrophic yeast Pichia pastoris and purified by heparin-Sepharose chromatography. Recombinant ghilanten-D1 inhibits bovine trypsin and human factor Xa with equilibrium inhibition constants (K(i)) of 126 and 1.2 nM, respectively. Ghilanten-D1 has been crystallized in complex with porcine beta-trypsin; three different-looking but isomorphous crystal forms were obtained, each belonging to the orthorhombic space group P2(1)2(1)2(1). These crystals diffracted to beyond 3.6 A resolution using a rotating-anode X-ray source. A data set complete to 3.7 A resolution was collected.
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