3.1.2.12	by the hanging drop vapor diffusion technique, to 2.2 A resolution. Crystals belong to space group P212121 with unit cell dimensions of a = 49.49 A, b = 129.75 A, c = 152.67 A, with 4 molecules per asymmetric unit	
3.1.2.12	by the sitting drop-vapor diffusion technique, at 2 A resolution. Crystals belong to space group P1 with unit cell dimensions a = 66.43 A, b = 68.95 A, c = 95.65 A, alpha = 92.41, beta = 99.79, gamma = 98.43. Contacts between the two monomers in the dimer are formed both by hydrogen bonds and salt bridges	
3.1.2.12	selenomethionine labelled recombinant enzyme, 30 mg/ml, hanging-drop vapor-diffusion method, 293K, precipitant solution: 16% PEG 4000, 0.2 M magnesium acetate, 0.2 M imidazole-malate, pH 6.5, 3% methanol, optimal crystals by microseeding, 1-5 d, production of selenomethionine-enzyme crystals is similar with 10% PEG 4000 and additional presence of 10 mM DTT, X-ray diffraction structure determination and analysis at 1.84 A resolution	
3.1.2.12	sitting drop vapour diffusion method, using 0.17 M ammonium acetate, 0.085 M sodium acetate trihydrate (pH 4.6), 25.5% (w/v) PEG 4000, and 15% (v/v) glycerol	
3.1.2.12	structure to 1.6 A resolution. A single dimer of FrmB is observed in the asymmetric unit. The overall fold of FrmB is characteristic of the alpha/beta-hydrolase fold