Publisher： John Wiley & Sons Inc
E-ISSN： 1744-3091|62|6|586-589
ISSN： 1744-3091
Source： Acta Crystallographica Section F, Vol.62, Iss.6, 2006-06, pp. : 586-589
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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 Å.
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