Chou_2008_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_64_1118

Reference

Title : Crystallization and preliminary X-ray diffraction analysis of phospholipase A1 isolated from hornet (Vespa basalis) venom - Chou_2008_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_64_1118
Author(s) : Chou CC , Hou MH
Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 64 :1118 , 2008
Abstract :

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.

PubMedSearch : Chou_2008_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_64_1118
PubMedID: 19052363
Gene_locus related to this paper: vesba-pa1

Related information

Gene_locus vesba-pa1
Structure 4QNN

Citations formats

Chou CC, Hou MH (2008)
Crystallization and preliminary X-ray diffraction analysis of phospholipase A1 isolated from hornet (Vespa basalis) venom
Acta Crystallographica Sect F Struct Biol Cryst Commun 64 :1118

Chou CC, Hou MH (2008)
Acta Crystallographica Sect F Struct Biol Cryst Commun 64 :1118