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Protein Science, Vol 3, Issue 12 2447-2449, Copyright © 1994 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Crystallization and preliminary X-ray analysis of glucose-fructose oxidoreductase from Zymomonas mobilis

H. LOOS, U. ERMLER, G. A. SPRENGER and H. SAHM
Institut fur Biotechnologie 1, Forschungszentrum Julich GmbH, P.O. Box 1913, D-52425 Julich, Germany

Glucose-fructose oxidoreductase (E.C. 1.1.99.-) from the ethanol-producing Gram-negative bacterium Zymomonas mobilis is a periplasmic, soluble enzyme that forms a homotetramer of 160 kDa with one NADP(H) cofactor per subunit that is tightly, but noncovalently, bound. The enzyme was crystallized by the hanging drop vapor diffusion method using sodium citrate as precipitant. The obtained crystals belong to the space group P2(1)2(1)2, with unit cell constants of 84.6 A, 94.1 A and 117.0 A, consistent with two monomers in the asymmetric unit. They diffract to a resolution of about 2 A and are suitable for X-ray structure determination.
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This article has been cited by other articles:


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 J. Biol. Chem.Home page
T. Wiegert, H. Sahm, and G. A. Sprenger
The Substitution of a Single Amino Acid Residue (Ser-116 right-arrow Asp) Alters NADP-containing Glucose-Fructose Oxidoreductase of Zymomonas mobilis into a Glucose Dehydrogenase with Dual Coenzyme Specificity
J. Biol. Chem., May 16, 1997; 272(20): 13126 - 13133.
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