PMID:8520491
| Citation |
Andersson, A, Schneider, G and Lindqvist, Y (1995) Purification and preliminary X-ray crystallographic studies of recombinant L-ribulose-5-phosphate 4-epimerase from Escherichia coli. Protein Sci. 4:1648-50 |
|---|---|
| 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. |
| Links |
PubMed PMC2143197 Online version:10.1002/pro.5560040823 |
| Keywords |
Base Sequence; Carbohydrate Epimerases/chemistry; Carbohydrate Epimerases/genetics; Carbohydrate Epimerases/isolation & purification; Crystallography, X-Ray; DNA Primers; Escherichia coli/enzymology; Escherichia coli/genetics; Molecular Sequence Data; Protein Conformation; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/isolation & purification |
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