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Purification and preliminary X‐ray crystallographic studies of recombinant L‐ribulose‐5‐phosphate 4‐epimerase from escherichia coli
Author(s) -
Andersson Arnold,
Schneider Gunter,
Lindqvist Ylva
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560040823
Subject(s) - escherichia coli , recombinant dna , ribulose , crystallography , chemistry , sodium formate , x ray crystallography , phosphate , enzyme , biochemistry , microbiology and biotechnology , rubisco , biology , gene , inorganic chemistry , diffraction , physics , optics
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‐ribuIose‐5‐phosphate 4‐epimerase, obtained with 4.0 M sodium formate as precipitant, belong to space group P42 1 2 with unit cell dimensions a = b = 107.8 Å and c = 281.4 Å and diffract to at least 2.2 Å resolution. Density measurements of these crystals are consistent with eight subunits in the asymmetric unit.