CRYSTALLIZATION AND PRELIMINARY-X-RAY CHARACTERIZATION OF A SOYBEAN SEED LIPOXYGENASE

[摘要] An isoenzyme of soybean (Glycine max L. Merrill cv. Provar) lipoxygenase (EC 1.13.11.12) has been crystallized using the vapor diffusion method. Crystals were grown from solutions of the protein (7 mg/ml) using 10 to 20 (w/v) polyethylene glycol 8000 in citrate/phosphate buffer (pH 5.7) containing 0.5% (w/v) n-octyl-.beta.-D-glucopyranoside. The crystals reached maximum dimensions of 0.3 mm .times. 0.2 mm .times. > 2 mm. The enzyme crystallized in space group C2221 with unit cell dimensions a = 246 .ANG., b = 193 .ANG. and c = 75 .ANG.. A calculated Vm value of 2.35 .ANG.3/dalton was obtained assuming two molecules per asymmetric unit. The density of the crystals was found to be 1.16 g/ml, which confirmed the presence of two molecules per asymmetric unit and indicated a solvent content of 47.5%.

[发布日期] 1990-02-20