Crystallization and preliminary X-ray characterization of a soybean seed lipoxygenase.
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 x 0.2 mm x greater than 2 mm. The enzyme crystallized in space group C222(1) with unit cell dimensions a = 246 A, b = 193 A and c = 75 A. A calculated Vm value of 2.35 A3/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%.
Stallings
W C
WC
Physical Sciences Center, Monsanto Company, St Louis, MO 63198.
Kroa
B A
BA
Carroll
R T
RT
Metzger
A L
AL
Funk
M O
MO
D050557:Catechol 2,3-Dioxygenase; D003460:Crystallization; D049308:Dioxygenases; D007527:Isoenzymes / Q000302:isolation & purification*; D010105:Oxygenases / Q000302:isolation & purification*; D011487:Protein Conformation; D012639:Seeds / Q000201:enzymology; D013025:Glycine max / Q000201:enzymology*; D014961:X-Ray Diffraction
D007527:Isoenzymes; D010105:Oxygenases; D049308:Dioxygenases; D050557:Catechol 2,3-Dioxygenase