2.8.1.10	C205S variant with a bound glycine imine intermediate, hanging drop vapor diffusion method, using 25% (w/v) PEG1500, 0.0125 M succinic acid, 0.044 M sodium dihydrogen phosphate, and 0.044 M glycine, pH 8.5	
2.8.1.10	native protein to 1.8 A resolution. Thi4 exists as an homooctamer with the disordered and largely hydrophilic N-terminal regions located on the exterior of the molecule. The octamer has the shape of a ring with flattened sides. Adenosine diphospho-5-(beta-ethyl)-4-methylthiazole-2-carboxylic acid is bound to the Thi4 active site, which is located near the inner ring of the octameric complex.. NAD is the most likely precursor	
2.8.1.10	structure of ThiG in complex with ThiS, the sulfur carrier protein, at 3.15 A resolution. Thiazole synthase is a tetramer with 222 symmetry. The monomer is a (betaalpha)8 barrel with similarities to the aldolase class 1 and flavin mononucleotide dependent oxidoreductase and phosphate binding superfamilies. The sulfur carrier protein ThiS is a compact protein with a fold similar to that of ubiquitin. Modeling the substrate, deoxy-D-xylulose 5-phosphate in the active site identifies Glu98 and Asp182 as active site residues likely to be involved in the catalysis of thiazole formation	
2.8.1.10	wild type enzyme complexed with ADP-ribulose, hanging drop vapor diffusion method, using 1.05 M potassium/sodium tartrate, 0.1 M CHES/sodium hydroxide, pH 9.5 and 0.2 M lithium sulfate	
2.8.1.10	wild type enzyme with bound glycine imine intermediate and iron, hanging drop vapor diffusion method, using 1.0 M sodium citrate, 0.1 M CHES/sodium hydroxide, pH 9.5