Otro
Crystallization and preliminary diffraction data of BaP1, a haemorrhagic metalloproteinase from Bothrops asper snake venom
Registro en:
Acta Crystallographica Section D-biological Crystallography. Copenhagen: Blackwell Munksgaard, v. 58, p. 1034-1035, 2002.
0907-4449
10.1107/S0907444902003633
WOS:000176271200016
WOS000176271200016.pdf
Autor
Watanabe, L.
Rucavado, A.
Kamiguti, A.
Theakston, RDG
Gutierrez, J. M.
Arni, R. K.
Resumen
BaP1 is a metalloproteinase isolated from the venom of the Central American snake Bothrops asper (terciopelo). It is a 24 kDa protein consisting of a single chain which includes the metalloproteinase domain only, therefore being classified as a class P-I snake-venom metalloproteinase. BaP1 induces prominent local tissue damage, such as haemorrhage, myonecrosis, blistering, dermonecrosis and oedema. In order to elucidate its structure, BaP1 was crystallized by the hanging-drop vapour-diffusion technique in 0.1 M bicine pH 9.0, 10% PEG 20 000 and 2%(v/v) dioxane. Diffraction data were observed to a resolution of 2.7 Angstrom. Crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 38.22, b = 60.17, c = 86.09 Angstrom.