title: Crystallization and preliminary X-ray diffraction analysis of transaldolase from Thermoplasma acidophilum.
abstract: 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 C222(1) with five monomers per asymmetric unit and crystal form 2 belonged to the monoclinic space group P2(1) with ten monomers per asymmetric unit.
authors.affiliation: Göttinger Zentrum für Molekulare Biowissenschaften, Georg-August-Universität Göttingen, Ernst-Caspari-Haus, Justus-von-Liebig-Weg 11, D-37077 Göttingen, Germany.
authors.forename: Anja
authors.initials: A
authors.lastname: Lehwess-Litzmann
authors.forename: Piotr
authors.initials: P
authors.lastname: Neumann
authors.forename: Ralph
authors.initials: R
authors.lastname: Golbik
authors.forename: Christoph
authors.initials: C
authors.lastname: Parthier
authors.forename: Kai
authors.initials: K
authors.lastname: Tittmann
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D013822:Thermoplasma / Q000201:enzymology*; D014153:Transaldolase / Q000737:chemistry*
chemical_list: D014153:Transaldolase