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Watanabe, L., Rucavado, A., Kamiguti, A., Theakston, R.David G., Gutierrez, J. M. and Arni, R. K. (2002) 'Crystallization and preliminary diffraction data of BaP1, a haemorrhagic metalloproteinase from Bothrops asper snake venom'. Acta Crystallographica Section D-Biological Crystallography, Vol 58, Issue 6, pp. 1034-1035.
Full text not available from this repository.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 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.
| Item Type: | Article |
|---|---|
| Subjects: | QU Biochemistry > Proteins. Amino Acids. Peptides > QU 58.5 DNA. WD Disorders of Systemic, Metabolic or Environmental Origin, etc > Animal Poisons > WD 410 Reptiles |
| Faculty: Department: | Groups (2002 - 2012) > Molecular & Biochemical Parasitology Group |
| Digital Object Identifer (DOI): | https://doi.org/10.1107/s0907444902003633 |
| Depositing User: | Lynn Roberts-Maloney |
| Date Deposited: | 09 Aug 2013 09:14 |
| Last Modified: | 06 Feb 2018 13:05 |
| URI: | https://archive.lstmed.ac.uk/id/eprint/3004 |
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