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Purification and Preliminary X-ray Crystallographic Studies of Recombinant L-ribulose-5-phosphate 4-epimerase from Escherichia Coli

Overview
Journal Protein Sci
Specialty Biochemistry
Date 1995 Aug 1
PMID 8520491
Citations 2
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Abstract

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.

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