Crystallization and preliminary X-ray data of chloromuconate cycloisomerase from Alcaligenes eutrophus JMP134 (pJP4)

J Mol Biol. 1993 Jul 5;232(1):305-7. doi: 10.1006/jmbi.1993.1385.


The pJP4-encoded chloromuconate cycloisomerase, an enzyme of the 2,4-dichlorophenoxy-acetate degradation pathway, was purified from cell-free extracts of Alcaligenes eutrophus JMP134 with a revised procedure. Tetragonal bipyramidal crystals were grown and characterized with respect to their X-ray diffraction properties. They were assigned to the space group I4, with cell dimensions of a = b = 111.9 A, c = 148.5 A. The crystals scattered to approximately 3 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcaligenes / enzymology*
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / ultrastructure
  • Crystallography
  • Intramolecular Lyases*
  • Isomerases / isolation & purification
  • Isomerases / ultrastructure*
  • X-Ray Diffraction


  • Bacterial Proteins
  • Isomerases
  • Intramolecular Lyases
  • chloromuconate cycloisomerase