Crystallization and preliminary X-ray diffraction analysis of phospholipase A1 isolated from hornet (Vespa basalis) venom

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 PLA1 from hornet venom with a molecular weight of 32 kDa are reported. PLA1 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 angstrom resolution at 100 K with an overall R-merge of 6.8%. The crystal belongs to the triclinic space group P1, with unit-cell parameters a = 57.2, b = 70.2, c = 81.6 angstrom, alpha = 107.0, beta = 109.9, gamma = 100.9 degrees. In each asymmetric unit, three or four subunits of PLA(1) are present according to the calculation of the solvent content.