3.5.3.6	-	209446, 209447, 685929	
3.5.3.6	apo-enzyme, sitting drop vapor diffusion method, using 0.9 M trisodium citrate, 0.1M sodium cacodylate pH 6.5	735070	
3.5.3.6	catalytically important residues are C406 and H278	652524	
3.5.3.6	crystal structure determination and analysis of purified recombinant enzyme at 1.6 and 2.0 A resolution, respectively	685929	
3.5.3.6	crystal structure determination and analysis of purified recombinant enzyme at 2.45 A resolution, recombinant selenomethionine-labeled enzyme by sitting drop vaour diffusion method	685929	
3.5.3.6	in complex with substrate	653916	
3.5.3.6	mutants C406A, H287A, D280A, and D166A in complex with L-arginine, protein solutions containing 20 mM arginine are mixed with an equal volume of mother liquor containing 34-38% 2-methyl-2,4-pentanediol, 6.0-7.0% PEG 3350, 0.1 M Tris-HCl, pH 7.6, and 20 mM arginine, equilibration against the mother liquor reservoir, 2-8 weeks, X-ray diffraction structure determination and anaylsis at 2.3-2.9 A resolution, modeling	680632	
3.5.3.6	sitting-drop vapor-diffusion technique at 23°C, apoPAD2 crystals with increasing concentrations of calcium (0-10 mM), 16 structures are solved at eight different calcium concentrations to 1.66-1.97 A	752353	
3.5.3.6	X-ray crystallographic coordinates for the structure of the C406A ADI -L-arginine complex, overview	687300