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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Base Sequence
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Carbohydrate Epimerases / chemistry*
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Carbohydrate Epimerases / genetics
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Carbohydrate Epimerases / isolation & purification*
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Crystallography, X-Ray
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DNA Primers
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Molecular Sequence Data
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Protein Conformation
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
Substances
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DNA Primers
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Recombinant Proteins
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Carbohydrate Epimerases
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L-ribulosephosphate 4-epimerase