Expression, purification and crystallization of a thermostable short-chain alcohol dehydrogenase from the archaeon Thermococcus sibiricus.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 6): 655-7, 2010 Jun 01.
Article
in En
| MEDLINE
| ID: mdl-20516592
Alcohol dehydrogenases belong to the oxidoreductase family and play an important role in a broad range of physiological processes. They catalyze the cofactor-dependent reversible oxidation of alcohols to the corresponding aldehydes or ketones. The NADP-dependent short-chain alcohol dehydrogenase TsAdh319 from the thermophilic archaeon Thermococcus sibiricus was overexpressed, purified and crystallized. Crystals were obtained using the hanging-drop vapour-diffusion method using 25%(w/v) polyethylene glycol 3350 pH 7.5 as precipitant. The crystals diffracted to 1.68 A resolution and belonged to space group I222, with unit-cell parameters a = 55.63, b = 83.25, c = 120.75 A.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Alcohol Dehydrogenase
/
Thermococcus
Language:
En
Journal:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Year:
2010
Document type:
Article
Affiliation country:
RUSSIA
Country of publication:
United kingdom