Crystallization and preliminary X-ray diffraction analysis of diaminopimelate epimerase from Escherichia coli

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):37-40. doi: 10.1107/S1744309109047708. Epub 2009 Dec 25.


Diaminopimelate (DAP) epimerase (EC 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Isomerases / chemistry*
  • Amino Acid Isomerases / isolation & purification
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / enzymology


  • Amino Acid Isomerases
  • diaminopimelate epimerase