Open AccessCrystallization and preliminary X‐ray diffraction analysis of diaminopimelate epimerase from Escherichia coli
Author(s) -
Hor Lilian,
Dobson Renwick C. J.,
Dogovski Con,
Hutton Craig A.,
Perugini Matthew A.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109047708
Subject(s) - escherichia coli , crystallization , resolution (logic) , lysine , molecular replacement , crystallography , chemistry , x ray crystallography , molecule , bacteria , diffraction , biosynthesis , stereochemistry , biochemistry , biology , physics , amino acid , enzyme , gene , organic chemistry , genetics , optics , artificial intelligence , computer science
Diaminopimelate (DAP) epimerase (EC 5.1.1.7) catalyzes the penultimate step of lysine biosynthesis in bacteria and plants, converting l , l ‐diaminopimelate to meso ‐diaminopimelate. Here, the cloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of DAP epimerase from Escherichia coli are presented. Crystals were obtained in space group P 4 1 2 1 2 and diffracted to 2.0 Å resolution, with unit‐cell parameters a = b = 89.4, c = 179.6 Å. Molecular replacement was conducted using Bacillus anthracis DAP epimerase as a search model and showed the presence of two molecules in the asymmetric unit, with an initial R free of 0.456 and R work of 0.416.