Open AccessCrystallization and preliminary X‐ray diffraction analysis of a novel Arg49 phospholipase A 2 homologue from Zhaoermia mangshanensis venom
Author(s) -
Murakami Mário T.,
Kuch Ulrich,
Mebs Dietrich,
Arni Raghuvir K.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107026073
Subject(s) - venom , phospholipase a2 , crystallization , diffraction , crystallography , residue (chemistry) , x ray , x ray crystallography , crystal structure , stereochemistry , chemistry , enzyme , materials science , biochemistry , physics , optics , organic chemistry
Zhaoermiatoxin, an Arg49 phospholipase A 2 homologue from Zhaoermia mangshanensis (formerly Trimeresurus mangshanensis , Ermia mangshanensis ) venom is a novel member of the PLA 2 ‐homologue family that possesses an arginine residue at position 49, probably arising from a secondary Lys49→Arg substitution that does not alter the catalytic inactivity towards phospholipids. Like other Lys49 PLA 2 homologues, zhaoermiatoxin induces oedema and strong myonecrosis without detectable PLA 2 catalytic activity. A single crystal with maximum dimensions of 0.2 × 0.2 × 0.5 mm was used for X‐ray diffraction data collection to a resolution of 2.05 Å using synchrotron radiation and the diffraction pattern was indexed in the hexagonal space group P 6 4 , with unit‐cell parameters a = 72.9, b = 72.9, c = 93.9 Å.