Expression, purification and preliminary crystallographic analysis of human sorbitol dehydrogenase.
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.
Darmanin
Connie
C
Department of Medicinal Chemistry, Victorian College of Pharmacy, Monash University (Parkville Campus), Parkville, Victoria 3052, Australia.
Iwata
Takeshi
T
Carper
Deborah A
DA
Sparrow
Lindsay G
LG
Chung
Roland P T
RP
El-Kabbani
Ossama
O
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
D018076:DNA, Complementary; D007064:L-Iditol 2-Dehydrogenase