Acta Crystallographica Section D

Biological Crystallography

Volume 58, Part 6 Number 2 (June 2002)

crystallization papers

Acta Cryst. (2002). D58, 1036-1038 [ doi:10.1107/S0907444902003645 ]

Crystallization of bothrombin, a fibrinogen-converting serine protease isolated from the venom of Bothrops jararaca

L. Watanabe, D. F. Vieira, R. K. Bortoleto and R. K. Arni

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 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 Å. The crystals belong to the space group P2₁2₁2₁, with unit-cell parameters a = 94.81, b = 115.68, c = 155.97 Å.

Keywords: snake venoms; bothrombin.