EC Number   |
|---|
    6.3.2.6 | - |
| 6.3.2.6 | at 2.5 A resolution |
| 6.3.2.6 | co-crystallization of SAICAR synthetase from Pyrococcus horikoshii with substrates and other nucleotides produces eight ligand bound structures, five in C2221 and three in H3 space groups. These ligand bound complexes have minor structural deviations compared to their corresponding apo structures. In most of the structures the hydrolyzed product of the nucleotide triphosphates are bound to the enzyme |
| 6.3.2.6 | crystals of SAICAR complexed with 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide and succinic acid are grown by hanging drop vapor diffusion at room temperature, mother liquor consists of 24 mg/ml SAICAR, 1 M ammonium sulfate, 100 mM 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide, 100 mM succinic acid and 50 mM Tris-HCl, pH 7.5, crystals diffract to 1.3 A |
| 6.3.2.6 | hanging drop vapor diffusion, drops contain protein at a concentration of 8-15 mg/ml in 50 mM Tris-HCl, pH 7.0, 40 mM aspartic acid and 1.0-1.25 M ammonium sulfate, crystals diffract to 1.9 A resolution |
| 6.3.2.6 | hanging-drop vapor diffusion, crystal structures of the ADP and the ADP/4-carboxy-5-aminoimidazole ribonucleotide complexes of SAICAR synthetase. ADP and 4-carboxy-5-aminoimidazole ribonucleotide bind to the active site in association with three Mg2+, two of which coordinate the same oxygen atom of the 4-carboxyl group of CAIR, whereas, the third coordinates the alpha- and beta-phosphoryl groups of ADP. The polypeptide fold for residues 204-221 of the Escherichia coli structure differs significantly from those of the ligand-free SAICAR synthetase from Thermatoga maritima and the adenine nucleotide complexes of the synthetase from Saccharomyces cerevisiae |
| 6.3.2.6 | hanging-drop vapor-diffusion conditions, 2.2 A resolution crystal structure. Protein structure is described and compared with that of the ATP-SAICAR synthase complex from yeast |
| 6.3.2.6 | hanging-drop vapor-diffusion method. Crystals of the complex of the enzyme SAICAR synthase with the reaction product belong to space group P2(1)2(1)2(1) containing one molecule per asymmetric unit |
| 6.3.2.6 | purified enzyme in 150 mM NaCl, 1 mM DTT, 10 mM HEPES-KOH, pH 7.5, is mixed with 50 mM Tris pH 8.0, 2M ammonium sulfate and 1% PEG400, X-ray diffraction structure determination and analysis at 2.8 A resolution, modeling |
| 6.3.2.6 | purified recombinant His-tagged enzyme complexed with ADP or ADP, L-Asp and 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, hanging drop vapour diffusion method, mixing of 0.002 ml of 0.25 mM protein in 15 mM Tris, pH 8.0, 25 mM KCl, 55 mM MgCl2, 5 mM EDTA, and 5 mM DTT, with 0.002 ml of reservoir solution containing 0.16 M sodium acetate, pH 4.5, 36-40% w/v PEG 200, plus mM ADP, 1 mM CAIR, and 4 mM Asp or plus 10 mM ADP, X-ray diffraction structure determination and analysis at 2.3-2.69 A resolution, modeling, molecular replacement using the Escherichia coli enzyme structure, PDB ID 2gqr, as search model |
