title: Crystallization and preliminary X-ray diffraction analysis of diaminopimelate epimerase from Escherichia coli.
abstract: 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 P4(1)2(1)2 and diffracted to 2.0 A resolution, with unit-cell parameters a = b = 89.4, c = 179.6 A. 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.
authors.affiliation: School of Chemistry, The University of Melbourne, Parkville, Victoria 3010, Australia.
authors.forename: Lilian
authors.initials: L
authors.lastname: Hor
authors.forename: Renwick C J
authors.initials: RC
authors.lastname: Dobson
authors.forename: Con
authors.initials: C
authors.lastname: Dogovski
authors.forename: Craig A
authors.initials: CA
authors.lastname: Hutton
authors.forename: Matthew A
authors.initials: MA
authors.lastname: Perugini
mesh_terms: D000591:Amino Acid Isomerases / Q000737:chemistry* / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology
chemical_list: D000591:Amino Acid Isomerases; C042032:diaminopimelate epimerase