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Crystallization and preliminary X‐ray diffraction analysis of a putative carbon–carbon bond hydrolase from Mycobacterium abscessus 103
Author(s) -
Zhang Zhang,
Jiang YongLiang,
Wu Yi,
He YongXing
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15001612
Subject(s) - crystallization , polyethylene glycol , hydrolase , chemistry , pseudomonas fluorescens , mycobacterium smegmatis , carbon fibers , crystallography , biology , materials science , biochemistry , enzyme , organic chemistry , bacteria , mycobacterium tuberculosis , medicine , tuberculosis , pathology , composite number , composite material , genetics
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 m M 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 P 2 1 , 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, V M was calculated to be 2.5 Å 3 Da −1 , which corresponds to a solvent content of 50%.