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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
16 mg/ml purified enzyme complexed with inhibitors acetate, flufenamic acid or indomethacin, hanging drop vapour diffusion method in 0.006 ml drops, 1:1 mixture of protein solution containing 10 mM potassium phosphate, pH 7.0, 1 mM DTT, 1 mM EDTA, 2 mM NADP+, with reservoir solution containing 25% w/v PEG 4000, 100 mM sodium citrate, pH 6.0, 2.5% v/v 2-methyl-2,4-pentanediol, and 800 mM ammonium acetate, 6 days to maximum size, X-ray diffraction structure determination of the complexes and analysis at 1.2-2.1 A resolution
20 mg/ml purified recombinant enzyme in a solution containing 1.4 mM PGD2 or inhibitor rutin, 1.2 mM NADP+ and NADPH, 50 mM MES, pH 6.0, and 25% w/v PEG 8000, hanging drop vapour diffusion method, 2-3 days, thick plate-shaped crystals of enzyme with NADP+ and PGD2 and of enzyme with NADPH and rutin, X-ray diffraction structure determination and analysis at 1.69 A resolution
in complex with bimatoprost and NADPH, hanging drop vapor diffusion method, using 1.0 mM BMP, 1.0 mM NADPH, 0.14 M NaCl, 50 mM MES buffer (pH 7.0), and 26% (w/v) PEG 8000
purified recombinant enzyme in complex with NADPH and bimatoprost BMP, an ocular hypotensive agent bound near the PGD2 binding site located on the alpha- and omega-chains, hanging drop vapour diffusion method, from 50 mM MES, pH 7.0, containing 7 mg/ml protein, 0.14 M NaCl, 26% w/v PEG 8000, 1.0 mM NADPH, and 1.0 mM BMP, added in a 95% ethanol solution, 4°C, 14 days, thick plate-shaped crystals, X-ray diffraction structure determination and analysis at 2.0 A resolution
purified recombinant apoenzyme or enzyme with bound cofactor NADPH, mixing of 20 mg/ml protein in 25 mM Tris, pH 8.0, 200 mM NaCl, 1% v/v glycerol, 1 mM TCEP with the reservoir solution containing 0.1 M sodium citrate pH 5.50, 20% PEG 3000 200 mM magnesium chloride, 100 mM Tris, pH 7.0, 10% PEG 8000 for apo- and complexed enzyme, 16°C, 2-4 weeks, X-ray diffraction structure determination and analysis at 1.8 A and 1.6 A resolution, respectively, molecular replacement
10 mg/ml purified recombinant enzyme from 0.1 M HEPES/NaOH, pH 7.5, 2.0 M ammonium sulfate, 5% w/v PEG 400, and 0.5 M NADPH by hanging drop vapour diffusion method, 20°C, 3 weeks, X-ray diffraction structure determination at room temperature and analysis at 2.6 A resolution
purified recombinant apoenzyme or enzyme with bound cofactor NADP+, mixing of 20 mg/ml protein in 25 mM Tris pH 8.0, 200 mM NaCl, 1% v/v glycerol, 1 mM TCEP with reservoir solution. For the apoenzyme, the reservoir solution contains 0.1 M MES-imidazole, pH 6.5, 10% PEG 20 000, 20% PEG 550 MME, 0.02 M glutamic acid, glycine, serine, alanine, and lysine, and for the cofactor complexed enzyme, it contains 0.2 M ammonium acetate, 0.1 M Bis-Tris pH 5.5, 25% PEG 3350, cryoprotectant is 15% ethylene glycol, 16°C, 2-4 weeks, X-ray diffraction structure determination and analysis at 1.25 A and 2.6 A resolution, respectively, molecular replacement