Crystallization of retinol dehydratase from Spodoptera frugiperda: improvement of crystal quality by modification by ethylmercurythiosalicylate

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.