Purification and preliminary X-ray crystallographic studies of recombinant L-ribulose-5-phosphate 4-epimerase from Escherichia coli. |
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| Authors: | A. Andersson G. Schneider Y. Lindqvist |
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| Affiliation: | Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, Sweden. |
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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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| Keywords: | araBAD operon crystallization L-ribulose-5-phosphate 4-epimerase X-ray crystallography |
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