Crystallization and preliminary x‐ray analysis of glucose‐fructose oxidoreductase from zymomonas mobilis
Protein Science, ISSN: 1469-896X, Vol: 3, Issue: 12, Page: 2447-2449
1994
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Article Description
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 P222, 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. Copyright © 1994 The Protein Society
Bibliographic Details
Wiley
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