1.1.1.103	apo form, in complex with NAD+ and glycerol, or with only NAD+, sitting drop vapor diffusion method, using 0.1 M HEPES (pH 7.0), 10% (w/v) PEG 4000, 10% (v/v) 2-propanol, or 0.2 M NaCl, 0.1 M HEPES (pH 7.5), 25% (w/v) PEG3350	738933	
1.1.1.103	at room temperature using hanging-drop vapour diffusion method, at 2.4 A resolution. The enzyme is a homotetramer, each monomer consisting of 350 amino acids that form two domains, a catalytic domain and a NAD+-binding domain, which contains an alpha/beta Rossmann fold motif. An extended twelve-stranded beta-sheet is formed by the association of pairs of monomers in the tetramer	699854	
1.1.1.103	by hanging-drop vapour-diffusion method, to 2.6 A resolution. Crystals grow in the tetragonal space group P43212, with unit-cell parameters a=b=124.5, c=271.1 A. There are four molecules in the asymmetric unit of the crystal	695358	
1.1.1.103	hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 and 0.2 M CaCl2	738606	
1.1.1.103	hanging-drop method	762567	
1.1.1.103	purified recombinant enzyme, hanging drop vapour diffusion method, 4°C, 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 0.0015 ml of protein and reservoir solution are mixed, the reservoir solution contains 0.2 M NaCl, 0.1 M HEPES, pH 7.5, and 40% v/v PEG 400, 5 days, X-ray diffraction structure determination and preliminary analysis at 2.2 A resolution	667071	
1.1.1.103	purified wild-type enzyme or enzyme mutant Y137F in complex with NAD+ and L-3-hydroxynorvaline or pyruvate or L-threonine, sitting drop vapor diffusion method, mixing of 0.001 ml of 40 mg/ml wild-type or 25 mg/ml mutant enzyme, and 1 mM NAD+ mixed with 0.001 ml of 100 mM cacodylate buffer, pH 6.4, 50% v/v 2-methyl-2,4-pentandiol, and 5% w/v PEG 8000, 20°C, crystals of ligand-bound wild-type or mutant enzymes by soaking the crystals in reservoir solution containing 0.3 M pyruvate for 2 h, or 0.1ML-threonine for 8 h or 0.1MDL-3-hydroxynorvaline for 7 h, respectively, X-ray diffraction structure determination and analysis at 1.77-2.07 A resolution, molecular replacement	722747	
1.1.1.103	selenomethionine-substituted enzyme, 10 mg/ml protein in 50 mM Tris-HCl buffer, pH 7.5, hanging-drop vapor-diffusion method at 4°C, mixing of 0.0015 ml of each, protein and reservoir solution, the latter containing 0.2 M sodium chloride, 0.1 M HEPES buffer, pH 7.5, and 40% v/v PEG 400, five days, X-ray diffraction structure determination and analysis, single wavelength anomalous diffraction method	688343	
1.1.1.103	sitting-drop vapor diffusion method at 4°C, crystal structures of the enzyme in apo, binary, and two ternary complexes (L-Ser- and L-Thr soaked forms) are determined at resolutions of 1.25-1.9 A	762728