Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties-5

<p><b>Copyright information:</b></p><p>Taken from "Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties"</p><p>http://www.biomedcentral.com/1472-6807/7/47</p><p>BMC Structural Biology 2007;7():47-47.</p><p>Published online 12 Jul 2007</p><p>PMCID:PMC1936996.</p><p></p> and EstE1(▯), in 20 mM potassium phosphate buffer (pH 7.0) were incubated at 80°C for the indicated times. Residual activities were then determined by measuring the amount of -nitrophenol released by esterase-catalyzed hydrolysis. The activity of a non-incubated sample was defined as 100