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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.

SUBMITTER: Lehwess-Litzmann A

PROVIDER: S-EPMC3087646 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of transaldolase from Thermoplasma acidophilum.

Lehwess-Litzmann Anja A Neumann Piotr P Golbik Ralph R Parthier Christoph C Tittmann Kai K

Acta crystallographica. Section F, Structural biology and crystallization communications 20110427 Pt 5

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 belo ...[more]

PMID: 21543867

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