2.7.4.22	apo-form UMPK, 2.35 A resolution, crystallisation is significantly improved in a strong magnetic field, buffer-screening procedure, 20 mM N-(2-acetamido)-2-iminodiacetic acid (ADA) pH 6.8, 5 mM beta-mercaptoethanol and 0.02% NaN3, sitting-drop vapour diffusion in 96-well plates, 100 K, monoclinic space group P212121, unit-cell paramerters a = 111.45, b = 120.07, c = 125.79A	690286	
2.7.4.22	bound to the UMP substrate, resolved at 2.3 A resolution, bound to the UDP product, resolved at 2.6 A resolution, bound to UTP, resolved at 2.45 A resolution	665637	
2.7.4.22	complexed with GTP, hanging drop vapor diffusion method, using 150 mM sodium acetate pH 4.8, 270 mM ammonium sulfate, 18% (w/v) PEG MME 550. Complexed with UDP, hanging drop vapor diffusion method, using 0.15 M sodium acetate pH 4.8, 0.35 M ammonium sulfate, 28% (w/v)PEG MME 550	721169	
2.7.4.22	D159N, hanging drop vapor diffusion method	698858	
2.7.4.22	of the apo-form, crystallization improves by a strong magnetic field, optimum buffer for solubilization is 20 mM N-(2-acetamido)iminodiacetic acid, pH 6.8, 0.02% NaN3 and 5 mM 2-mercaptoethanol	671130	
2.7.4.22	purified recombinant enzyme in complex with ATP, 300 nl sitting drops containing 1.5 mg/mL purified protein are mixed with 3.3 mM ATP, 0.33 mM MgCl2, 66 mM Li2SO4, 3% PEG 3000, 33 mM imidazole, pH 8.0, and 20 mM spermine tetrahydrochloride, equilibration against a reservoir solution of 200 mM Li2SO4, 10% PEG 3000, and 100 mM imidazole, pH 8.0, cryoprotection in 70% reservoir solution with 30% glycerol, 2 days, X-ray diffraction structure determination and analysis at 2.82 A resolution	693652	
2.7.4.22	purified recombinant enzyme, X-ray diffraction structure determination and analysis at 2.5 A resolution	692284	
2.7.4.22	purified recombinant SeMet-substituted apo-enzyme XC1936, crystallization in a strong magnetic field, protein in 5 mM 2-mercaptoethanol, 100 mM N-(2-acetamido)-2-iminodiacetic acid, pH 6.8, and 0.02% NaN3, optimization of the reservoir solution, 25°C, X-ray diffraction structure determination and analysis at 2.35 A resolution	671130	
2.7.4.22	purified recombinant UMP kinase mutant D159N, bound to GTP, by hanging drop vapour diffusion method, 0.004 ml of protein solution containing 4 mg/ml UMPK mutant in 50 mM Tris-HCl, pH 8.0, and 100 mM NaCl, mixed with 0.004 ml precipitant solution containing 22.5 mM GTP and 21.5% w/v PEG 400 in 100 mM sodium acetate, pH 4.6, equilibration against reservoir solution containing 43% PEG 400, 20°C, X-ray diffraction structure determination and analysis at 2.8-3.0 A resolution, molecular replacement and structure modelling	698858	
2.7.4.22	resolved at 2.4 A resolution. Complexed with AMP-PNP, resolved at 3 A resolution. Complexed with AMP-PNP and UMP, resolved at 2.55 A resolution	666054	
2.7.4.22	ternary complex with UMP and the nonhydrolyzable ATP analogue alpha,beta-methylene-ATP (SsUMPK-UMP-AMPPCP), resolution 2.1 A, a complex with UMP (SsUMPK-UMP), resolution 2.2 A, a complex with UTP (SsUMPK-UTP), resolution 2.8 A, hanging drop vapor diffusion, protein solution (2UL) in 10 mM TRIS/Cl pH 7.6 with 4.6 mg/ml SSUMPK and 2 mM UMP and 5 mM MgCl2 mixed with 2 UL mother solution (0.65 M sodium acetate, 100 mM CdCl2, 0.1 M HEPES), pH 7.5	672233	
2.7.4.22	UMP kinase in complex with ATP and Mg2+ at 2.82 A resolution, 0.2 M lithium sulfate, 10% polyethylene glycol 3000, 0.1 M imidazole, pH 8.0, space group P 61 2 2, allosteric nucleotide-binding site identified, a structural model for the allosteric regulation presented	693652	
2.7.4.22	UMPK with N-terminal His-tag, in complex with a phosphate ion, co-crystallized with UMP, and UTP, cross-talk region between two subunits of UpUMPK is identified, vapor diffusion, hanging drop, 0.2 m ammonium fluoride and 20% (w/v) poly(ethylene glycol) 3350, 15°C, enzyme concentration is 1.8 mg/ml, 5 mM GTP, resolution of 2.5 A, space group P 1 21 1, cell dimensions a =79.8, b = 96.6, c = 96.3 A, beta = 105.8	692284	
2.7.4.22	using sodium/potassium tartrate (1.2 M) at pH 7.4 and 10 mM GTP	723289	
2.7.4.22	with ATP and UMP, with UMP, with UTP	672233