Crystallization and preliminary crystallographic analysis of NAD+-preferring aldohexose dehydrogenase from the thermoacidophilic archaeon Thermoplasma acidophilum.Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 01; 62(Pt 6):586-9.AC
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.
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MeSH
Pub Type(s)
Journal Article
Research Support, Non-U.S. Gov't
Language
eng
PubMed ID
16754989
Citation
Yasutake, Yoshiaki, et al. "Crystallization and Preliminary Crystallographic Analysis of NAD+-preferring Aldohexose Dehydrogenase From the Thermoacidophilic Archaeon Thermoplasma Acidophilum." Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, vol. 62, no. Pt 6, 2006, pp. 586-9.
Yasutake Y, Nishiya Y, Tamura N, et al. Crystallization and preliminary crystallographic analysis of NAD+-preferring aldohexose dehydrogenase from the thermoacidophilic archaeon Thermoplasma acidophilum. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006;62(Pt 6):586-9.
Yasutake, Y., Nishiya, Y., Tamura, N., & Tamura, T. (2006). Crystallization and preliminary crystallographic analysis of NAD+-preferring aldohexose dehydrogenase from the thermoacidophilic archaeon Thermoplasma acidophilum. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 62(Pt 6), 586-9.
Yasutake Y, et al. Crystallization and Preliminary Crystallographic Analysis of NAD+-preferring Aldohexose Dehydrogenase From the Thermoacidophilic Archaeon Thermoplasma Acidophilum. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt 6):586-9. PubMed PMID: 16754989.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR
T1 - Crystallization and preliminary crystallographic analysis of NAD+-preferring aldohexose dehydrogenase from the thermoacidophilic archaeon Thermoplasma acidophilum.
AU - Yasutake,Yoshiaki,
AU - Nishiya,Yoshiaki,
AU - Tamura,Noriko,
AU - Tamura,Tomohiro,
Y1 - 2006/05/31/
PY - 2006/03/03/received
PY - 2006/05/11/accepted
PY - 2006/6/7/pubmed
PY - 2006/8/5/medline
PY - 2006/6/7/entrez
SP - 586
EP - 9
JF - Acta crystallographica. Section F, Structural biology and crystallization communications
JO - Acta Crystallogr Sect F Struct Biol Cryst Commun
VL - 62
IS - Pt 6
N2 - 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.
SN - 1744-3091
UR - https://www.unboundmedicine.com/medline/citation/16754989/Crystallization_and_preliminary_crystallographic_analysis_of_NAD+_preferring_aldohexose_dehydrogenase_from_the_thermoacidophilic_archaeon_Thermoplasma_acidophilum_
DB - PRIME
DP - Unbound Medicine
ER -