2.4.2.19	-	
2.4.2.19	apo, quinolinate-bound, 5-phospho-alpha-D-ribose 1-diphosphate-bound, and phthalate-bound forms. Crystallized at room temperature by the hanging drop vapor diffusion method. Both apo and holo crystals belong to space group R32 (alpha = 90°, beta = 90°, and gamma = 120°). One molecule per asymmetric unit except in QAPRTase holophthalate crystals where two molecules are found. The unit cell dimensions are: a = b = 154.9 A and c = 68.9 A (apo), a = b = 154.8 A and c = 68.6 A (holoquinolinate), a = b = 154.9 A and c = 70.6 A (holo-5-phospho-alpha-D-ribose 1-diphosphate), a = b = 155.5 A and c = 121.1 A (holophthalate), a = b = 154.7 A and c = 69.3 A (holophthalate-5-phospho-alpha-D-ribose 1-diphosphate)	
2.4.2.19	apoenzyme and in complex with phthalic acid, sitting drop vapor diffusion method, using 50 mM MES pH 6.5, 0.1 M NaH2PO4, 0.1 M K H2PO4, and 1.6-2.1 M NaCl	
2.4.2.19	apoenzyme and in complex with quinolinic acid or nicotinic acid mononucleotide, hanging drop vapor diffusion method, using	
2.4.2.19	crystal structure of Hp-QAPRTase with bound quinolinic acid, nicotinic acid mononucleotide, and phthalic acid. Hp-QAPRTase crystals are grown at 20°C using the hanging drop vapor diffusion method	
2.4.2.19	hangig-drop vapor diffusion method, X-ray crystal structure of the apoenzyme is determined by multiple isomorphous replacement at 2.4 A resolution, complex with quinolinate, phthalate, nicotinate mononucleotideand ternary complex with phthalate and a substrate analog 5-phosphoribosyl-1-(beta-methylene)diphosphate	
2.4.2.19	hanging or sitting drop vapor diffusion method, using 0.48 M ammonium sulfate, 25% (w/v) PEG 6000 and 0.1 M bis-Tris (pH 6.5)	
2.4.2.19	hanging-drop vapor-diffusion method	
2.4.2.19	hanging-drop vapor-diffusion method, determination of crystal structure of the enzyme with bound quinolinate to 2.8 A resolution and with bound nicotinic acid mononucleotide	
2.4.2.19	hanging-drop vapour-diffusion method, PEG 8000	
2.4.2.19	hanging-drop vapour-diffusion method, PEG MME 2K	
2.4.2.19	in complex with nicotinate mononucleotide, hanging drop vapor diffusion method, using 100 mM Tris-HCl, pH 8.0, 16-24% (w/v) PEG 8000, 150-200 mM ammonium acetate	
2.4.2.19	PDB code: 2jbm (apo-hQPRTase), alpha/beta barrel fold (12 beta strands + 11 alpha helices) with N-terminal domain (residues 1-112, 279-291) and C-terminal domain (residues 113-278), similar to bacterial QPRTases (PDB: 1x1o), active site at alpha/beta open sandwich structure that faces an alpha/beta barrel of the adjacent subunit harbouring the quinolinic acid binding site (Arg102, Arg138, Arg161, Lys139, Lys171, pocket at the centre of the barrel), space group P2(1)2(1)2(1), unit-cell parameters: a = 111.5 A, b = 179.5 A, c = 194.7 A, 12 monomers in asymmetric unit arranged as 2 hexamers of D3 symmetry, sitting-drop vapour diffusion: 5 days, 20°C, 2 microlitre protein solution (10 mg/ml, pH7.5) + 2 microlitre precipitant (0.6 M potassium/sodium tartrate, 0.1 M sodium HEPES pH7.6), resolution of 2 A, phase determination using multiple wavelength anomalous diffraction on crystals of the Se-Met variant	
2.4.2.19	purified recombinant enzyme, hanging drop vapour diffusion method, 10 mg/ml protein, crystallization solution contains 10% PEG 6000, and 0.1 M MES, pH 6.0, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement, model construction