Open AccessCrystallization and preliminary X‐ray diffraction analysis of myotoxin I, a Lys49‐phospholipase A 2 from Bothrops moojeni
Author(s) -
MarchiSalvador D. P.,
Silveira L. B.,
Soares A. M.,
Fontes M. R. M.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910502717x
Subject(s) - bothrops , phospholipase a2 , snake venom , myotoxin , molecule , chemistry , crystallography , venom , stereochemistry , enzyme , biochemistry , organic chemistry
A new myotoxic Lys49‐phospholipase A 2 isolated from Bothrops moojeni snake venom has been crystallized. The crystals diffracted to 2.18 Å resolution using a synchrotron‐radiation source and belong to space group C 2. The unit‐cell parameters are a = 56.8, b = 125.0, c = 64.7 Å, β = 105.5°. Preliminary analysis indicates the presence of four molecules in the asymmetric unit. This may suggest a new quaternary structure for this Lys49‐phospholipase A 2 in contrast to the dimeric and monomeric structures solved so far for this class of proteins.