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- W1994188510 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 Å. Crystals belong to space group P212121, with unit-cell parameters a = 38.22, b = 60.17, c = 86.09 Å." @default.
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- W1994188510 date "2002-05-29" @default.
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- W1994188510 title "Crystallization and preliminary diffraction data of BaP1, a haemorrhagic metalloproteinase from<i>Bothrops asper</i>snake venom" @default.
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- W1994188510 doi "https://doi.org/10.1107/s0907444902003633" @default.
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