Zhang_2015_Acta.Crystallogr.F.Struct.Biol.Commun_71_239

The PhlG protein from Mycobacterium abscessus 103 (mPhlG), which shares 30% sequence identity with phloretin hydrolase from Eubacterium ramulus and 38% sequence identity with 2,4-diacetylphloroglucinol hydrolase from Pseudomonas fluorescens Pf-5, is a putative carbon-carbon bond hydrolase. Here, the expression, purification and crystallization of mPhlG are reported. Crystals were obtained using a precipitant consisting of 100 mM citric acid pH 5.0, 1.0 M lithium chloride, 8%(w/v) polyethylene glycol 6000. The crystals diffracted to 1.87 A resolution and belonged to space group P21, with unit-cell parameters a = 71.0, b = 63.4, c = 74.7 A, alpha = 90.0, beta = 103.2, gamma = 90.0 degrees . Assuming the presence of two mPhlG molecules in the asymmetric unit, VM was calculated to be 2.5 A(3) Da(-1), which corresponds to a solvent content of 50%.