Crystallization of retinol dehydratase from Spodoptera frugiperda: Improvement of crystal quality by modification by ethylmercurythiosalicylate
Abstract
Retinol dehydratase is a sulfotransferase which is presumed to catalyze the dehydration of its substrate via a transient retinyl sulfate intermediate. Crystals (space group P21, unit-cell parameters a = 82.05, b = 66.61, c = 84.90 Å, β = 111.29°) are significantly improved by covalent modification of the protein with ethylmercury.
This paper has been withdrawn.