Open AccessCrystallization and preliminary X‐ray diffraction analysis of transaldolase from Thermoplasma acidophilum
Author(s) -
LehwessLitzmann Anja,
Neumann Piotr,
Golbik Ralph,
Parthier Christoph,
Tittmann Kai
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111009274
Subject(s) - thermoplasma acidophilum , transaldolase , crystallization , x ray crystallography , materials science , crystallography , diffraction , chemistry , biochemistry , organic chemistry , physics , optics , pentose phosphate pathway , enzyme , glycolysis
The metabolic enzyme transaldolase from Thermoplasma acidophilum was recombinantly expressed in Escherichia coli and could be crystallized in two polymorphic forms. Crystals were grown by the hanging‐drop vapour‐diffusion method using PEG 6000 as precipitant. Native data sets for crystal forms 1 and 2 were collected in‐house to resolutions of 3.0 and 2.7 Å, respectively. Crystal form 1 belonged to the orthorhombic space group C 222 1 with five monomers per asymmetric unit and crystal form 2 belonged to the monoclinic space group P 2 1 with ten monomers per asymmetric unit.