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Title: Crystallization and preliminary X-ray diffraction analysis of a novel Arg49 phospholipase A{sub 2} homologue from Zhaoermia mangshanensis venom

Journal Article · · Acta Crystallographica. Section F
 [1]; ;  [2]
  1. Department of Physics, UNESP-State University of São Paulo, São José do Rio Preto 15054-000 (Brazil)
  2. Zentrum der Rechtsmedizin, Klinikum der Johann Wolfgang Goethe-Universität, Kennedyallee 104, D-60596 Frankfurt am Main (Germany)

A single crystal of zhaoermiatoxin 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 P6{sub 4}, with unit-cell parameters a = 72.9, b = 72.9, c = 93.9 Å. Zhaoermiatoxin, an Arg49 phospholipase A{sub 2} homologue from Zhaoermia mangshanensis (formerly Trimeresurus mangshanensis, Ermia mangshanensis) venom is a novel member of the PLA{sub 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{sub 2} homologues, zhaoermiatoxin induces oedema and strong myonecrosis without detectable PLA{sub 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 P6{sub 4}, with unit-cell parameters a = 72.9, b = 72.9, c = 93.9 Å.

OSTI ID:
22360375
Journal Information:
Acta Crystallographica. Section F, Vol. 63, Issue Pt 7; Other Information: PMCID: PMC2335147; PMID: 17620723; PUBLISHER-ID: pu5189; OAI: oai:pubmedcentral.nih.gov:2335147; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English