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Title: Crystallization and preliminary crystallographic analysis of NAD{sup +}-preferring aldohexose dehydrogenase from the thermoacidophilic archaeon Thermoplasma acidophilum

Journal Article · · Acta Crystallographica. Section F
 [1];  [2];  [1];  [1]
  1. 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)
  2. Tsuruga Institute of Biotechnology, Toyobo Co. Ltd, 10-24 Toyo-cho, Tsuruga 914-0047 (Japan)

NAD{sup +}-preferring aldohexose dehydrogenase from the thermoacidophilic archaeon T. acidophilum was crystallized using the hanging-drop vapour-diffusion technique and X-ray diffraction data were collected to a resolution of 2.8 Å. 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{sup +} rather than NADP{sup +} 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 Å.

OSTI ID:
22360215
Journal Information:
Acta Crystallographica. Section F, Vol. 62, Issue Pt 6; Other Information: PMCID: PMC2243078; PMID: 16754989; PUBLISHER-ID: bw5142; OAI: oai:pubmedcentral.nih.gov:2243078; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English