Gf. Audette et al., Crystallization and preliminary X-ray diffraction studies of monomeric isocitrate dehydrogenase from Corynebacterium glutamicum, ACT CRYST D, 55, 1999, pp. 1584-1585
A monomeric isocitrate dehydrogenase has been crystallized for the first ti
me. This enzyme catalyzes the conversion of isocitrate to oxalosuccinate an
d subsequently to alpha-ketoglutarate and CO2; the coenzyme NADP(+) is redu
ced to NADPH during the reaction. Polyethylene glycol 2000 monomethyl ether
was used to crystallize the enzyme in space group CZ with unit-cell parame
ters a = 137.1, b = 54.6, c = 126.4 Angstrom beta = 108.2 degrees. The very
small crystal (0.05 x 0.20 x 0.05 mm) diffracted to 3.5 Angstrom d spacing
using synchrotron radiation.