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 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 A 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 A, 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.
Chou
Chia-Cheng
CC
National Synchrotron Radiation Research Center, Hsinchu 300, Taiwan.
Hou
Ming-Hon
MH
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D019476:Insect Proteins / Q000737:chemistry*; D054466:Phospholipases A1 / Q000737:chemistry* / Q000302:isolation & purification; D014862:Wasp Venoms / Q000201:enzymology*; D014863:Wasps / Q000201:enzymology* / Q000378:metabolism; D014961:X-Ray Diffraction
D019476:Insect Proteins; D014862:Wasp Venoms; D054466:Phospholipases A1