Publication Date:
2015-01-28
Description:
The PhlG protein fromMycobacterium abscessus103 (mPhlG), which shares 30% sequence identity with phloretin hydrolase fromEubacterium ramulusand 38% sequence identity with 2,4-diacetylphloroglucinol hydrolase fromPseudomonas fluorescensPf-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 mMcitric acid pH 5.0, 1.0 Mlithium chloride, 8%(w/v) polyethylene glycol 6000. The crystals diffracted to 1.87 Å resolution and belonged to space groupP21, with unit-cell parametersa= 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,VMwas calculated to be 2.5 Å3 Da−1, which corresponds to a solvent content of 50%.
Electronic ISSN:
2053-230X
Topics:
Biology
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Chemistry and Pharmacology
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Geosciences
,
Physics
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