3.2.1.145	purified recombinant enzyme, vapour diffusion method, mixing of 0.001 ml of 80 mg/ml protein in 0.02 M HEPES, pH 7.5, and 0.15 M NaCl, with 0.001 ml of reservoir solution containing 0.05 M calcium chloride dihydrate,0.1 M bis-Tris pH 6.5, 30% v/v polyethylene glycol monomethyl ether 550, and equilibration against 80.00 ml of reservoir solution, 17°C, X-ray diffraction structure determination and analysis at 1.4 A resolution, molecular replacement using using domain I of the Bacteroides thetaiotaomicron glycosyl hydrolase as search model, PDB ID 3nqh, modelling	
3.2.1.145	purified recombinant His-tagged wild-type and selenomethionine-labeled enzymes in complex with galactose, IPTG, galactan, and lactose, hanging drop vapor diffusion method, mixing of 0.001 ml of 50 mg/ml protein in a buffer containing 20 mM Tris-HCl, pH 8.0, and 100 mM NaCl, with 0.001 ml of reservoir solution containing 100 mM sodium acetate, pH 4.5, and 2.9-3.3 M sodium chloride,16°C, 3 days, X-ray diffraction structure determination and analysis at 2.7-3.2 A resolution	
3.2.1.145	selenomethionine-labeled recombinant Pc1,3Gal43A, hanging-drop vapour-diffusion method, 25°C, the reservoir solution contains 16% w/v PEG 10000, 95 mM ammonium sulfate, 95 mM Bis-Tris, pH 5.5, and 4.8% v/v glycerol, 3-10 days, X-ray diffraction structure determination and analysis at 1.8 A resolution, multiwavelength anomalous dispersion method, since molecular replacement is unsuccessful