Open AccessCrystallization and preliminary X‐ray diffraction analysis of phospholipase A 1 isolated from hornet ( Vespa basalis ) venom
Author(s) -
Chou ChiaCheng,
Hou MingHon
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108030182
Subject(s) - venom , crystallization , triclinic crystal system , crystallography , solvent , phospholipase , phospholipase a2 , chemistry , stereochemistry , biology , crystal structure , biochemistry , enzyme , organic chemistry
Phospholipase A 1 (PLA 1 ) isolated from the black‐bellied hornet ( Vespa basalis ) catalyzes the hydrolysis of emulsified phospholipids in addition to the potent haemolytic activity responsible for its lethal effect. In this study, the crystallization and preliminary crystallographic analysis of PLA 1 from hornet venom with a molecular weight of 32 kDa are reported. PLA 1 was crystallized at 277 K using PEG 4000 as precipitant and a 96.5% complete native data set was collected from a frozen crystal to 2.5 Å resolution at 100 K with an overall R merge of 6.8%. The crystal belongs to the triclinic space group P 1, with unit‐cell parameters a = 57.2, b = 70.2, c = 81.6 Å, α = 107.0, β = 109.9, γ = 100.9°. In each asymmetric unit, three or four subunits of PLA 1 are present according to the calculation of the solvent content.