Author:
Iermak Iuliia,Degtjarik Oksana,Steffler Fabian,Sieber Volker,Kuta Smatanova Ivana
Abstract
The glyceraldehyde dehydrogenase fromThermoplasma acidophilum(TaAlDH) is a microbial enzyme that catalyzes the oxidation of D-glyceraldehyde to D-glycerate in the artificial enzyme cascade designed for the conversion of glucose to the organic solvents isobutanol and ethanol. Various mutants ofTaAlDH were constructed by a random approach followed by site-directed and saturation mutagenesis in order to improve the properties of the enzyme that are essential for its functioning within the cascade. Two enzyme variants, wild-typeTaAlDH (TaAlDHwt) and an F34M+S405N variant (TaAlDH F34M+S405N), were successfully crystallized. Crystals ofTaAlDHwt belonged to the monoclinic space groupP1211 with eight molecules per asymmetric unit and diffracted to a resolution of 1.95 Å.TaAlDH F34M+S405N crystallized in two different space groups: triclinicP1 with 16 molecules per asymmetric unit and monoclinicC121 with four molecules per asymmetric unit. These crystals diffracted to resolutions of 2.14 and 2.10 Å for theP1 andC121 crystals, respectively.
Publisher
International Union of Crystallography (IUCr)
Subject
Condensed Matter Physics,Genetics,Biochemistry,Structural Biology,Biophysics
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