Purification, crystallization and preliminary crystallographic analysis of a lipase from Proteus sp.K107
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Abstract
After induced by IPTG, the recombinant E.coli expressed Lipase LipK107 as HisX6 fusion protein.High purity enzyme was obtained by affinity chromatography and gel filtration chromatography.Purified lipase was analyzed by circular dichrosim (CD) in order to reveal the secondary structure composition of lipase LipK107.Then, purified lipase was crystallized by the hanging-drop vapour-diffusion method.High quality crystals were obtained using 0.1mol/L sodium citrate tribasic dihydrate pH6.2, 10% v/v 2-propanol, 15% w/v polyethylene glycol 4000 as precipitant.X-ray diffraction data was collected to 2.0 using synchrotron radiation.
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