4.2.1.104	-	
4.2.1.104	enzyme SpCynS as DNA-protein complex is crystallized as an impurity and its identity is determined using mass-spectrometric analysis. The crystals seems to have a ligand bound in the active site, glycerol molecules are bound at the entry to the active site of the enzyme. Mixing of 500 nl of 5.5 mg/ml protein-DNA complex in 20 mM MES potassium, pH 6.5, 60 mM KCl, 5 mM MgCl2, 2 mM DTT, with 500 nl of reservoir solution containing 0.1 M HEPES, pH 7.5, 2% v/v 2-propanol, 0.1 M sodium acetate, 18% w/v PEG 8000, and equilibration against 0.055 ml of reservoir solution, four months at 20°C, X-ray diffraction structure determination and analysis at 2.1 A resolution, the cryoprotecting solution consists of mother liquor containing 25% v/v glycerol, the crystals belong to space group P1, molecular replacement solution using the target DNA-protein complex or its components as a search model and the EcCynS crystal structure (PDB ID 1dw9) as a search model, modeling without ligand	
4.2.1.104	purified recombinant MBP-tagged enzyme, sitting drop vapor diffusion method, 13 mg/ml protein solution is mixed with crystallization solution, containing 0.1 M Tris, pH 7.5, 15% w/v PEG 6000, in a 1:1 ratio, about 2 months, room temperature, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement using the crystal structure of Escherichia coli cyanase (PDB ID 2IV1) as the starting model	
4.2.1.104	selenomethionine-labeled purified recombinant enzyme, also crystals of enzyme with complexed inhibitors oxalate and chloride, 2 mM dithiothreitol, sitting drop vapour diffusion method, from 2.1 M ammonium sulfate, 50 mM Na2KPO4, pH 7.3, microseeding with large sitting drops at 18°C with wild-type crystals, 5-7 days, X-ray diffraction structure determinzation and analysis at 1.65 A resolution by multiwavelength anomalous diffraction MAD method