Watanabe, L.Vieira, D. F.Bortoleto, R. K.Arni, R. K.2014-05-202014-05-202002-06-01Acta Crystallographica Section D-biological Crystallography. Copenhagen: Blackwell Munksgaard, v. 58, p. 1036-1038, 2002.0907-4449http://hdl.handle.net/11449/21953Bothrombin, a snake-venom serine protease, specifically cleaves fibrinogen, releasing fibrinopeptide A to form non-crosslinked soft clots, aggregates platelets in the presence of exogeneous 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 Angstrom. 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 Angstrom.1036-1038engArtigo10.1107/S0907444902003645WOS:000176271200017Acesso abertoWOS000176271200017.pdf91625089789458870000-0003-2460-1145