【摘 要】
：
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-diacetylphloroglucino
【机 构】
：
MOE Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou Unive
【出 处】
：
The 9th Asian Biophysics Association Symposium (ABA2015)(第九届
论文部分内容阅读
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 unitcell parameters a =71.0, b =63.4, c =74.7 (A), a =90.0, β =103.2, y =90.0°.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％.
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