title: Crystallization and preliminary diffraction data of BaP1, a haemorrhagic metalloproteinase from Bothrops asper snake venom.
abstract: 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.
authors.affiliation: Department of Physics, IBILCE/UNESP, CP 136, Sao José do Rio Preto, CEP 15054-000, Brazil.
authors.forename: L
authors.initials: L
authors.lastname: Watanabe
authors.forename: A
authors.initials: A
authors.lastname: Rucavado
authors.forename: A
authors.initials: A
authors.lastname: Kamiguti
authors.forename: R D G
authors.initials: RD
authors.lastname: Theakston
authors.forename: J M
authors.initials: JM
authors.lastname: Gutiérrez
authors.forename: R K
authors.initials: RK
authors.lastname: Arni
mesh_terms: D000818:Animals; D017837:Bothrops; D003435:Crotalid Venoms / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008666:Metalloendopeptidases / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D003435:Crotalid Venoms; D008666:Metalloendopeptidases; C069317:hemorrhagic metalloproteinase