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Crystallization behaviour of glyceraldehyde dehydrogenase from Thermoplasma acidophilum
Author(s) -
Iermak Iuliia,
Degtjarik Oksana,
Steffler Fabian,
Sieber Volker,
Kuta Smatanova Ivana
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15020270
Subject(s) - thermoplasma acidophilum , triclinic crystal system , monoclinic crystal system , glyceraldehyde , dehydrogenase , crystallography , stereochemistry , crystallization , chemistry , enzyme , molecule , biochemistry , organic chemistry , crystal structure
The glyceraldehyde dehydrogenase from Thermoplasma acidophilum ( Ta AlDH) 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 of Ta AlDH 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‐type Ta AlDH ( Ta AlDHwt) and an F34M+S405N variant ( Ta AlDH F34M+S405N), were successfully crystallized. Crystals of Ta AlDHwt belonged to the monoclinic space group P 12 1 1 with eight molecules per asymmetric unit and diffracted to a resolution of 1.95 Å. Ta AlDH F34M+S405N crystallized in two different space groups: triclinic P 1 with 16 molecules per asymmetric unit and monoclinic C 121 with four molecules per asymmetric unit. These crystals diffracted to resolutions of 2.14 and 2.10 Å for the P 1 and C 121 crystals, respectively.