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Updated: Aug 10, 2026

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
Published on: December 1, 2020
Crystallization and preliminary X-ray diffraction studies of monomeric isocitrate dehydrogenase from Corynebacterium
G F Audette1, J W Quail, K Hayakawa
1Department of Biochemistry, University of Saskatchewan, 107 Wiggins Road, Saskatoon SK, S7K 5E5, Canada.
Abstract:
A monomeric isocitrate dehydrogenase has been crystallized for the first time. This enzyme catalyzes the conversion of isocitrate to oxalosuccinate and subsequently to alpha-ketoglutarate and CO(2); the coenzyme NADP(+) is reduced to NADPH during the reaction. Polyethylene glycol 2000 monomethyl ether was used to crystallize the enzyme in space group C2 with unit-cell parameters a = 137.1, b = 54.6, c = 126.4 A, beta = 108.2 degrees. The very small crystal (0. 05 x 0.20 x 0.05 mm) diffracted to 3.5 A d spacing using synchrotron radiation.

