title: Expression, purification and preliminary crystallographic analysis of human sorbitol dehydrogenase.
abstract: Human sorbitol dehydrogenase (SDH) was expressed in Escherichia coli BL21 cells and purified using ammonium sulfate precipitation and anion-exchange and dye-affinity chromatography. Purified SDH was crystallized from polyethylene glycol solutions using the hanging-drop vapour-diffusion method. X-ray data were collected to 2.75 A resolution. The crystals belong to the monoclinic C2 space group, with unit-cell parameters a = 145.9, b = 52.3, c = 169.0 A, beta = 101.8 degrees. This is the first crystallization report of human sorbitol dehydrogenase.
authors.affiliation: Department of Medicinal Chemistry, Victorian College of Pharmacy, Monash University (Parkville Campus), Parkville, Victoria 3052, Australia.
authors.forename: Connie
authors.initials: C
authors.lastname: Darmanin
authors.forename: Takeshi
authors.initials: T
authors.lastname: Iwata
authors.forename: Deborah A
authors.initials: DA
authors.lastname: Carper
authors.forename: Lindsay G
authors.initials: LG
authors.lastname: Sparrow
authors.forename: Roland P T
authors.initials: RP
authors.lastname: Chung
authors.forename: Ossama
authors.initials: O
authors.lastname: El-Kabbani
mesh_terms: D018360:Crystallography, X-Ray; D018076:DNA, Complementary / Q000096:biosynthesis; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007064:L-Iditol 2-Dehydrogenase / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D008099:Liver / Q000378:metabolism
chemical_list: D018076:DNA, Complementary; D007064:L-Iditol 2-Dehydrogenase