Figure 4From: Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability propertiesAnalysis of wild-type and mutant EstE1 by gel filtration chromatography. Purified EstE1 proteins were loaded onto a Superdex 200 column and eluted as described in Methods. Estimated molecular weights of wild-type EstE1 (●), EstE1F276A (■), EstE1F276E (□), EstE1V274A (▲), EstE1V274A/F276A (▯), EstE1L299D (▼), EstE1R270A (▯), EstE1E295A (▯), and EstE1R270A/E295A (▯) are presented. Molecular mass standards (albumin, 67 kDa; ovalbumin, 43 kDa; and chymotrypsinogen A, 25 kDa) were subjected to the same process, and their migration is indicated.Back to article page