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Figure 4 | BMC Structural Biology

Figure 4

From: Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties

Figure 4

Analysis 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.

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