Crystallization and preliminary diffraction data of BaP1, a haemorrhagic metalloproteinase from Bothrops asper snake venom

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorWatanabe, L.
dc.creatorRucavado, A.
dc.creatorKamiguti, A.
dc.creatorTheakston, RDG
dc.creatorGutierrez, J. M.
dc.creatorArni, R. K.
dc.date2014-05-20T14:02:17Z
dc.date2014-05-20T14:02:17Z
dc.date2002-06-01
dc.date.accessioned2017-04-05T21:27:06Z
dc.date.available2017-04-05T21:27:06Z
dc.identifierActa Crystallographica Section D-biological Crystallography. Copenhagen: Blackwell Munksgaard, v. 58, p. 1034-1035, 2002.
dc.identifier0907-4449
dc.identifierhttp://hdl.handle.net/11449/21952
dc.identifier10.1107/S0907444902003633
dc.identifierWOS:000176271200016
dc.identifierWOS000176271200016.pdf
dc.identifierhttp://dx.doi.org/10.1107/S0907444902003633
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/867432
dc.descriptionBaP1 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.
dc.languageeng
dc.publisherBlackwell Munksgaard
dc.relationActa Crystallographica Section D: Biological Crystallography
dc.rightsinfo:eu-repo/semantics/openAccess
dc.titleCrystallization and preliminary diffraction data of BaP1, a haemorrhagic metalloproteinase from Bothrops asper snake venom
dc.typeOtro


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