Crystallization and preliminary X-ray data of chloromuconate cycloisomerase from Alcaligenes eutrophus JMP134 (pJP4).
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.
Hammer
A
A
Institut für Organische Chemie und Isotopenforschung, Universität Stuttgart, Federal Republic of Germany.
Hildenbrand
T
T
Hoier
H
H
Ngai
K L
KL
Schlömann
M
M
Stezowski
J J
JJ
D000421:Alcaligenes / Q000201:enzymology*; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000648:ultrastructure; D003461:Crystallography; D019753:Intramolecular Lyases; D007535:Isomerases / Q000302:isolation & purification / Q000648:ultrastructure*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D007535:Isomerases; D019753:Intramolecular Lyases; C055773:chloromuconate cycloisomerase