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 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.
Pakhomova
S
S
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA.
Luz
J G
JG
Kobayashi
M
M
Mellman
D
D
Buck
J
J
Newcomer
M E
ME
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
D001565:Benzoates; D005035:Ethylmercury Compounds; C418469:ethylmercury thiosalicylate; D013849:Thimerosal; D006836:Hydro-Lyases; C100603:retinol dehydratase