Crystallization and preliminary diffraction data of BaP1, a haemorrhagic metalloproteinase from Bothrops asper snake venom.
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 A. Crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 38.22, b = 60.17, c = 86.09 A.
Watanabe
L
L
Department of Physics, IBILCE/UNESP, CP 136, Sao José do Rio Preto, CEP 15054-000, Brazil.
Rucavado
A
A
Kamiguti
A
A
Theakston
R D G
RD
Gutiérrez
J M
JM
Arni
R K
RK
D000818:Animals; D017837:Bothrops; D003435:Crotalid Venoms / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008666:Metalloendopeptidases / Q000737:chemistry*; D011487:Protein Conformation
D003435:Crotalid Venoms; D008666:Metalloendopeptidases; C069317:hemorrhagic metalloproteinase