Open AccessPurification, crystallization and preliminary X‐ray diffraction analysis of crotamine, a myotoxic polypeptide from the Brazilian snake Crotalus durissus terrificus
Author(s) -
Coronado Mônika A.,
Georgieva Dessislava,
Buck Friedrich,
Gabdoulkhakov Azat H.,
Ullah Anwar,
Spencer Patrick J.,
Arni Raghuvir K.,
Betzel Christian
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112032721
Subject(s) - crotalus , orthorhombic crystal system , venom , molecular replacement , chemistry , molecule , crystallization , stereochemistry , crystallography , biochemistry , crystal structure , organic chemistry
Crotamine, a highly basic myotoxic polypeptide (molecular mass 4881 Da) isolated from the venom of the Brazilian rattlesnake Crotalus durissus terrificus , causes skeletal muscle contraction and spasms, affects the functioning of voltage‐sensitive sodium channels by inducing sodium influx and possesses antitumour activity, suggesting potential pharmaceutical applications. Crotamine was purified from C. durissus terrificus venom; the crystals diffracted to 1.9 Å resolution and belonged to the orthorhombic space group I 2 1 2 1 2 1 or I 222, with unit‐cell parameters a = 67.75, b = 74.4, c = 81.01 Å. The self‐rotation function indicated that the asymmetric unit contained three molecules. However, structure determination by molecular replacement using NMR‐determined coordinates was unsuccessful and a search for potential derivatives has been initiated.