3.2.1.99	-	
3.2.1.99	crystallization is performed by the sitting-drop vapour-diffusion method. Single crystals are obtained from a solution containing 0.1 M MES buffer pH 6.5, 0.8 M ammonium sulfate, 0.1 M EDTA, 0.1 M L-proline and 5% (v/v) dioxane. X-ray diffraction data are collected to a resolution of 2.86 A using synchrotron radiation. The diffraction pattern is indexed in the tetragonal space group P422, with unit-cell parameters a = b = 83.71, c = 408.25 A	
3.2.1.99	hanging drop vapour-diffusion	
3.2.1.99	hanging-drop vapor-diffusion method using 1.0 mM sodium citrate as a precipitant at pH 6.0. Structure determined at 1.9 A to an R-factor of 18.3% and an R-free-factor of 22.5%. The enzyme molecule has a five-bladed beta-propeller fold. Crystals belong to orthorhombic space group P2(1)2(1)2(1) with unit cell parameters of a = 40.3, b = 77.8 and c = 89.7 A	
3.2.1.99	native and seleno-methionine-labelled derivative, by sitting-drop vapour-diffusion method, to 1.9 and 2.7 A resolution, respectively. Native protein crystals appear in two different space groups, P1, with unit-cell parameters a=51.9, b=57.6, c=86.2 A, alpha=82.3, beta=87.9, gamma=63.6, and P212121, with unit-cell parameters a=57.9, b=163.3, c=202.0 A. The selenol-methionine-labelled derivative of Abn2 only crystallizes in one crystal form, which is similar to the form of space group P212121 of the wild-type protein, with unit-cell parameters a=57.84, b=163.22, c=201.85 A, which can accommodate four molecules (each containing 13 selenomethionine residues) in the asymmetric unit	
3.2.1.99	preliminary x-ray analysis	
3.2.1.99	purified recombinant His-tagged enzyme, 0.0005 ml of protein solution containing 30 mg/ml in 25 mM Tris-HCl buffer, pH 7, 5, is mixed with 0.0005 ml of reservoir solution containing 0.1 M MES buffer, pH 6.5, 0.8 M ammonium sulfate, 0.1 M EDTA, 0.1 M L-proline and 5% v/v dioxane, X-ray diffraction structure determination and analysis at 2.86 A resolution	
3.2.1.99	purified recombinant wild-type enzyme, and mutant enzyme E201A in complex with arabinotriose, hanging drop vapour diffusion, 0.0025-0.003 ml of protein solution with 6.5-13 mg/ml protein is mixed with an equal volume of precipitant solution containing 1.7 M lithium sulfate, 0.1 M Tris buffer, pH 7.5, and 15% v/v glycerol for the wild-type enzyme, and 1.9 M lithium sulfate, 0.1 M Tris buffer, pH 8.5, and 4% w/v PEG 400 for the mutant enzyme, X-ray diffraction structure determination and analysis, molecular replacement	
3.2.1.99	resolution limit of 3.5 A	
3.2.1.99	sitting drop vapor diffusion method, using 65% (w/v) 2-methyl-2,4-pentadiol and 100 mM Tris, pH 8.5	
3.2.1.99	sitting-drop vapor-diffusion method at 20°C. Crystal structures of inactive mutant enzymes D27A and D147N, are determined in complex with arabino-oligosaccharides	
3.2.1.99	vapor diffusion method, using 10 mM NiCl2, 100 mM tris(hydroxymethyl)aminomethane-HCl pH 8.5, and 20% PEG 2000 monomethyl ether