title: Crystallization and preliminary crystallographic analysis of NAD+-preferring aldohexose dehydrogenase from the thermoacidophilic archaeon Thermoplasma acidophilum.
abstract: 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.
authors.affiliation: 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.
authors.forename: Yoshiaki
authors.initials: Y
authors.lastname: Yasutake
authors.forename: Yoshiaki
authors.initials: Y
authors.lastname: Nishiya
authors.forename: Noriko
authors.initials: N
authors.lastname: Tamura
authors.forename: Tomohiro
authors.initials: T
authors.lastname: Tamura
mesh_terms: 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
chemical_list: D019843:Archaeal Proteins; D012997:Solvents; D009243:NAD; D002237:Carbohydrate Dehydrogenases; C501231:aldohexose dehydrogenase