Crystallization and preliminary crystallographic analysis of monodehydroascorbate radical reductase from cucumber.

Satoshi Sano, You-Na Kang, Hiroko Shigemizu, Nobuhiko Morishita, Hye-Jin Yoon, Kazumi Saito, Kozi Asada, Bunzo Mikami

Laboratory of Chemistry of Biological Function, Graduate School of Agriculture, Kyoto Prefectural University, Shimogamo, Sakyo, 606-8522, Japan.

Acta crystallographica. Section D, Biological crystallography 2004 Aug

filter terms:

Monodehydroascorbate (MDA) radical reductase (EC 1.6.5.4) is an FAD enzyme that catalyzes the univalent reduction of MDA radical to ascorbate using NAD(P)H as an electron donor. The recombinant MDA reductase from cucumber was crystallized using polyethylene glycol 6000 as a precipitant. The crystals belong to space group P2(1), with unit-cell parameters a = 60.8, b = 138.6, c = 61.7 A, beta = 114.5 degrees, and contained two molecules per asymmetric unit. The Matthews coefficient (VM) and the solvent content are 2.46 A3 Da(-1) and 50.0%, respectively. Diffraction data were collected to a resolution of 2.4 A at 100 K using Cu Kalpha radiation with a multi-wire area detector and gave a data set with an overall Rsym of 10.0% and a completeness of 92.5%.

Citation

Satoshi Sano, You-Na Kang, Hiroko Shigemizu, Nobuhiko Morishita, Hye-Jin Yoon, Kazumi Saito, Kozi Asada, Bunzo Mikami. Crystallization and preliminary crystallographic analysis of monodehydroascorbate radical reductase from cucumber. Acta crystallographica. Section D, Biological crystallography. 2004 Aug;60(Pt 8):1498-9