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Updated: Aug 22, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
Structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 A resolution
Eric L Wise1, Julie Akana, John A Gerlt
1Deparment of Biochemistry, University of Wisconsin, Madison, WI 53706, USA.
Abstract:
The crystal structure of D-ribulose 5-phosphate 3-epimerase (RPE) from the cyanobacterium Synechocystis was determined by X-ray crystallography to 1.6 A resolution. The enzyme, which catalyzes the epimerization of D-ribulose 5-phosphate and D-xylulose 5-phosphate, assembles as a hexamer of (beta/alpha)(8)-barrels in the crystallographic asymmetric unit. The active site is highly similar to those of two previously reported RPEs and provides further evidence for essential catalytic roles for several active-site residues.
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