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Journal Article

Crystallization and preliminary x‐ray analysis of glucose‐fructose oxidoreductase from zymomonas mobilis

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Ermler,  Ulrich       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Loos, H., Ermler, U., Sprenger, G. A., & Sahm, H. (1994). Crystallization and preliminary x‐ray analysis of glucose‐fructose oxidoreductase from zymomonas mobilis. Protein Science, 3(12), 2447-2449. doi:10.1002/pro.5560031228.


Cite as: https://hdl.handle.net/21.11116/0000-0008-390D-B
Abstract
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 homotet‐ramer 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 P21212, with unit cell constants of 84.6 Å, 94.1 Å, and 117.0 Å, consistent with two monomers in the asymmetric unit. They diffract to a resolution of about 2 Å and are suitable for X‐ray structure determination.