Expression, purification and preliminary crystallographic analysis of phosphoribosyl isomerase (PriA) from Streptomyces coelicolor

Authors: Wright, Helena; Barona-Gómez, Francisco; Hodgson, David A.; Fülöp, Vilmos

Source: Acta Crystallographica Section D, Volume 60, Number 3, March 2004 , pp. 534-536(3)

Publisher: Blackwell Publishing

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Abstract:

The priA gene encoding the enzyme phosphoribosyl isomerase from Streptomyces coelicolor, a novel bifunctional enzyme involved in both histidine and tryptophan biosynthesis, was heterologously expressed and purified in Escherichia coli as an N-terminal His-tag fusion. The purified recombinant enzyme was crystallized using the hanging-drop method in 1.50 M ammonium sulfate and 100 mM sodium citrate pH 4.8. Crystals were obtained of up to 0.05 × 0.05 × 0.3 mm in size. A full data set to 2 Å resolution was collected at the ESRF beamline ID14-1 and space group P3_1,221 was assigned, with unit-cell parameters a = 65.1, c = 104.7 Å.

Keywords: phosphoribosyl isomerase; bifunctional enzyme; histidine and tryptophan biosynthesis

Document Type: Research article

DOI: 10.1107/S0907444903028877

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