Crystallization and preliminary crystallographic analysis of NAD+-preferring aldohexose dehydrogenase from the thermoacidophilic archaeon Thermoplasma acidophilum.
The aldohexose dehydrogenase from the thermoacidophilic archaeon Thermoplasma acidophilum (AldT) is a 28 kDa molecular-weight enzyme that catalyzes the oxidation of various aldohexoses, with a preference for NAD+ rather than NADP+ as a cofactor. The recombinant AldT was crystallized using the hanging-drop vapour-diffusion technique at 293 K under several acidic conditions with polyethylene glycol (PEG) and ammonium sulfate as precipitants. Optimization of the initial crystallizations conditions yielded single crystals in solution containing 0.1 M sodium acetate pH 4.6, 18%(w/v) PEG 4000, 0.2 M ammonium sulfate and 15%(v/v) glycerol. An X-ray diffraction data set was collected to a resolution of 2.8 A.
Yasutake
Yoshiaki
Y
Research Institute of Genome-based Biofactory, National Institute of Advanced Industrial Science and Technology (AIST), 2-17-2-1 Tsukisamu-Higashi, Toyohira-ku, Sapporo 062-8517, Japan.
Nishiya
Yoshiaki
Y
Tamura
Noriko
N
Tamura
Tomohiro
T
D019843:Archaeal Proteins / Q000737:chemistry; D002237:Carbohydrate Dehydrogenases / Q000737:chemistry*; D003460:Crystallization / Q000379:methods; D009243:NAD; D012997:Solvents; D013822:Thermoplasma / Q000201:enzymology*; D014961:X-Ray Diffraction
D019843:Archaeal Proteins; D012997:Solvents; D009243:NAD; D002237:Carbohydrate Dehydrogenases; C501231:aldohexose dehydrogenase