CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE FROM ZYMOMONAS-MOBILIS

Glucose-fructose oxidoreductase (E.C.1.1.99.-) from the ethanol-produc ing Gram-negative bacterium Zymomonas mobilis is a periplasmic, solubl e enzyme that forms a homotetramer of 160 kDa with one NADP(H) cofacto r per subunit that is tightly, but noncovalently, bound. The enzyme wa s crystallized by the hanging drop vapor diffusion method using sodium citrate as precipitant. The obtained crystals belong to the space gro up P2(1)2(1)2, with unit cell constants of 84.6 Angstrom, 94.1 Angstro m, and 117.0 Angstrom, consistent with two monomers in the asymmetric unit. They diffract to a resolution of about 2 Angstrom and are suitab le for X-ray structure determination.