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

Crystals of phospholipase A₁ from hornet (V. basalis) venom were obtained that diffracted X-rays to a resolution of at least 2.5 Å resolution. Phospholipase A₁ (PLA₁) 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 Å 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 Å, α = 107.0, β = 109.9, γ = 100.9°. In each asymmetric unit, three or four subunits of PLA₁ are present according to the calculation of the solvent content