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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Crystallization of bothrombin, a fibrinogen-converting serine protease isolated from the venom of Bothrops jararaca. Watanabe, L., Vieira, D.F., Bortoleto, R.K., Arni, R.K. Acta Crystallogr. D Biol. Crystallogr. (2002) [Pubmed]
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