title: 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 P2(1), unit-cell parameters a = 82.05, b = 66.61, c = 84.90 A, beta = 111.29 degrees ) are significantly improved by covalent modification of the protein with ethylmercury.
authors.affiliation: Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA.
authors.forename: S
authors.initials: S
authors.lastname: Pakhomova
authors.forename: J G
authors.initials: JG
authors.lastname: Luz
authors.forename: M
authors.initials: M
authors.lastname: Kobayashi
authors.forename: D
authors.initials: D
authors.lastname: Mellman
authors.forename: J
authors.initials: J
authors.lastname: Buck
authors.forename: M E
authors.initials: ME
authors.lastname: Newcomer
mesh_terms: D000818:Animals; D001565:Benzoates / Q000737:chemistry*; D003460:Crystallization; D005035:Ethylmercury Compounds / Q000737:chemistry*; D006836:Hydro-Lyases / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D018411:Spodoptera / Q000201:enzymology*; D013849:Thimerosal; D014961:X-Ray Diffraction
chemical_list: D001565:Benzoates; D005035:Ethylmercury Compounds; C418469:ethylmercury thiosalicylate; D013849:Thimerosal; D006836:Hydro-Lyases; C100603:retinol dehydratase