Purification and Preliminary X-ray Crystallographic Studies of Recombinant L-ribulose-5-phosphate 4-epimerase from Escherichia Coli
Overview
Authors
Affiliations
The araD gene from Escherichia coli, coding for L-ribulose-5-phosphate 4-epimerase, was overexpressed and the resulting enzyme was purified to homogeneity. Crystals of L-ribulose-5-phosphate 4-epimerase, obtained with 4.0 M sodium formate as precipitant, belong to space group P4212 with unit cell dimensions a = b = 107.8 A and c = 281.4 A and diffract to at least 2.2 A resolution. Density measurements of these crystals are consistent with eight subunits in the asymmetric unit.
Li J, Xie Z, Wang M, Ai G, Chen Y PLoS One. 2015; 10(3):e0120542.
PMID: 25822496 PMC: 4425429. DOI: 10.1371/journal.pone.0120542.
Bourand A, Yebra M, Boel G, Maze A, Deutscher J J Bacteriol. 2013; 195(11):2652-61.
PMID: 23564164 PMC: 3676056. DOI: 10.1128/JB.02276-12.