Crystallization and preliminary X-ray diffraction analysis of a putative carbon–carbon bond hydrolase from Mycobacterium abscessus 103

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 Å resolution and belonged to space group P21, with unit-cell parameters a = 71.0, b = 63.4, c = 74.7 Å, α = 90.0, β = 103.2, γ = 90.0°. Assuming the presence of two mPhlG molecules in the asymmetric unit, VM was calculated to be 2.5 Å3 Da−1, which corresponds to a solvent content of 50%.

Source: Acta Crystallographica Section F - January 28, 2015 Category: Biochemistry Authors: Zhang, Z.Jiang, Y.-L.Wu, Y.He, Y.-X. Tags: PhlG carbon – carbon bond hydrolase Mycobacterium abscessus 103 research communications Source Type: research