2.3.1.179	crystal structure determination and analysis at 2.6 A resolution	
2.3.1.179	hanging drop vapor diffusion method. 1.3 A resolution crystal structure	
2.3.1.179	hanging drop vapour diffusion method at room temperature, using 27% PEG 8000 as precipitant and buffered at pH 7.5 with 0.1 M HEPES. Crystal structure is determined with the multiple isomorphous replacement method and refined at 2.4 A resolution, space group P3(1)21	
2.3.1.179	hanging-drop vapour-diffusion method	
2.3.1.179	purified recombinant enzyme, hanging drop vapour diffusion technique, mixing of 0.0015 ml of 21 mg/ml protein solution with an equal amount of reservoir solution, containing 0.2 M lithium chloride, 0.1 M HEPES sodium salt pH 7.0, and 24% PEG 6000, and equilibration against 0.3 ml of reservoir solution, 13°C, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement using the enzyme structure of Escherichia coli, PDB ID 1KAS, as search model	
2.3.1.179	purified recombinant free wild-type enzyme, and mutant C164Q enzyme, free or in complex with 3-(benzoylamino)-2-hydroxybenzoic acid, mixing of 0.001 ml of 20 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 150 mM NaCl, with 0.001 ml reservoir solution containing 0.2 M MgCl2, 0.1 M Tris-HCl, pH 7.0, 10% w/v PEG 8000 for the wild-type enzyme, or 0.001 ml of 20 mg/ml protein in 50 mM Na2HPO4, pH 7.8, 150 mM NaCl, 10% v/v glycerol, and 0.5 mM DTT with 0.001 ml of reservoir consisting of 0.2 M NH4HCO2, 25% w/v PEG 3350 for the mutant enzyme, equilibration against 0.06 ml reservoir solution, at 20°C, X-ray diffraction structure determination and analysis at 1.67-2.46 A resolution, molecular replacement	
2.3.1.179	purified recombinant mutant H303A from 20% polyethylene glycol 3350, 0.2 M potassium acetate, X-ray diffraction structure determination and analysis	
2.3.1.179	purified recombinant wild-type and mutant E383A enzymes, hanging-drop vapour-diffusion method at room temperature, 0.001 ml of protein solution, containing 10 mg/ml
protein in 20 mM Tris-HCl, pH 8.0, 50 mM NaCl, and 10% glycerol, is mixed with 0.001 ml of precipitating solution, containing 0.2 M sodium acetate, 0.1 M Tris-HCl, pH 8.5, and 30% PEG 4000, formation of different crystal forms, X-ray diffraction structure determinations and analysis at 1.3-2.1 A resolution	
2.3.1.179	rod-shaped crystals of the purified enzyme are grown in two weeks by the hanging-drop vapor-diffusion method, 1.54 A resolution, space group P3(1)21, cells dimensions: a = b = 100.8 A, c = 74.7 A	
2.3.1.179	sitting drop vapor diffusion method, using either 0.1 M sodium chloride, 0.1 M bicine pH 9.0, 20% (w/v) PEG MME 550 or 0.1 M HEPES pH 7.5, 12% (w/v) PEG 3350 or 0.1 M Bis-Tris pH 5.5, 25% (w/v) PEG 3350, 0.2 M ammonium sulfate