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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 01;67(Pt 5):584-6. Epub 2011 Apr 27

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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 Ã, 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.

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

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