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Tagatose-1,6-bisphosphate aldolase (EC 4.1.2.40) is situated at the branching of the tagatose-6-phosphate and Embden-Meyerhof-Parnas (glycolysis) metabolic pathways, where it catalyzes the reversible cleavage of tagatose-1,6-bisphosphate to dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. The recombinant protein from Streptococcus pyogenes was overexpressed in Escherichia coli in its native and selenomethionine-derivative forms and purified using ion-exchange and hydrophobic interaction chromatography. Orthorhombic crystals suitable for structural analysis were obtained by the hanging-drop vapour-diffusion method for both isoforms. The crystals belong to space group P212121, with unit-cell parameters a = 63.7, b = 108.1, c = 238.7 Å for the native form and a = 64.1, b = 108.3, c = 239.8 Å for the selenomethionine derivative. The asymmetric unit contains four protomers, corresponding to a crystal volume per protein weight (VM) of 2.8 Å3 Da-1 and a solvent content of 56% by volume.

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Portable Document Format (PDF) file https://doi.org/10.1107/S0907444903028427/pu5032sup1.pdf
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