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  • Title: Crystallization of bothrombin, a fibrinogen-converting serine protease isolated from the venom of Bothrops jararaca.
    Author: Watanabe L, Vieira DF, Bortoleto RK, Arni RK.
    Journal: Acta Crystallogr D Biol Crystallogr; 2002 Jun; 58(Pt 6 Pt 2):1036-8. PubMed ID: 12037309.
    Abstract:
    Bothrombin, a snake-venom serine protease, specifically cleaves fibrinogen, releasing fibrinopeptide A to form non-crosslinked soft clots, aggregates platelets in the presence of exogenous fibrinogen and activates blood coagulation factor VIII. Bothrombin shares high sequence homology with other snake-venom proteases such as batroxobin (94% identity), but only 30 and 34% identity with human alpha-thrombin and trypsin, respectively. Single crystals of bothrombin have been obtained and X-ray diffraction data have been collected at the Laboratorio Nacional de Luz Sincrotron to a resolution of 2.8 A. The crystals belong to the space group P2(1)2(1)2(1), with unit-cell parameters a = 94.81, b = 115.68, c = 155.97 A.
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