UNSPECIFIED. (2004) Expression, purification and preliminary crystallographic analysis of phosphoribosyl isomerase (PriA) from Streptomyces coelicolor. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 60 (Part 3). pp. 534-536. ISSN 0907-4449

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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 0.05x0.05x0.3 mm in size. A full data set to 2 Angstrom resolution was collected at the ESRF beamline ID14-1 and space group P3(1,2)21 was assigned, with unit-cell parameters a=65.1, c=104.7 Angstrom.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology
Journal or Publication Title:	ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
Publisher:	BLACKWELL MUNKSGAARD
ISSN:	0907-4449
Date:	March 2004
Volume:	60
Number:	Part 3
Number of Pages:	3
Page Range:	pp. 534-536
Identification Number:	10.1107/S0907444903028877
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/8750

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