EC Number   |
|---|
    3.1.3.2 | - |
| 3.1.3.2 | apo-enzyme or in complex with L-(+)-tartrate, hanging drop vapor diffusion method, using 0.2 M sodium formate, 17% m(w/v) PEG 3350, 0.025% (w/v) low gelling temperature agarose, or 0.1 M Tris pH 8.5, 21% (w/v) PEG 6000, 0.025% (w/v) low gelling temperature agarose, respectively |
| 3.1.3.2 | AtTLP18.3 proteins are crystallized by the hanging drop vapor diffusion method at 23°C. X-ray crystallography reveal the folding of AtTLP18.3 as a three-layer sandwich with 3 alpha-helices in the upper layer, 4 beta-sheets in the middle layer, and 2 alpha-helices in the lower layer, which resembles a Rossmann fold |
| 3.1.3.2 | complexed with the inhibitor L(+)-tartrate, sitting drop vapor diffusion method, using 20% (w/v) PEG 3350 and 0.2 M sodium acetate at pH 4.5 |
| 3.1.3.2 | crystal structures of a substrate-trapping mutant P4 enzyme complexed with nicotinamide mononucleotide, 5'-AMP, 3'-AMP, and 2'-AMP. The structures reveal an anchor-shaped substrate-binding cavity comprising a conserved hydrophobic box that clamps the nucleotide base, a buried phosphoryl binding site, and three solvent-filled pockets that contact the ribose and the hydrogen-bonding edge of the base. Two solvent-filled pockets flanking the ribose are key to the dual recognition of 5'-nucleotides and 3'-nucleotides. These pockets minimize the enzyme's direct interactions with the ribose and provide sufficient space to accommodate 5' substrates in an anti conformation and 3' substrates in a syn conformation |
| 3.1.3.2 | hanging drop vapour diffusion method, co-crystallization of PAP in the presence of 50 mM NaF |
| 3.1.3.2 | in complex with orthovanadate, using polyethylene glycol 1500 as the precipitating agent |
| 3.1.3.2 | purified enzyme, 22 mg/ml protein in 0.1 M acetate, pH 4.9, mixed with well solution containing 0.1 M citric acid, pH 3.5-4.0, 7.5% PEG 6000, 10% isopropanol, 50 mM phosphate, and 10% glycerol, 4°C, cryoprotection by increase of glycerol concentration to 20%, X-ray diffraction structure determination and analysis at 2.5 A resolution |
| 3.1.3.2 | purified recombinant AphA in complex with adenosine and phosphate, with dCMP, or with osmate, sitting drop method, 0.002 ml protein solution containing 10 mg/ml protein in sodium acetate buffer, pH 7.0, mixed with 0.1 ml of precipitant solution containing 17-22% w/v PEG 6000, and 1 mM MgCl2, 20°C, equilibration against 2 ml of precipitant solution, soaking in ligand solution containing 50 mM sodium acetate, pH 7.0, 35% w/v PEG 6000, and 50 mM ligand for ligand complexing, derivatizing with Au and spermine, X-ray diffraction structure determination and analysis at 1.25-2.14 A resolution |
| 3.1.3.2 | recombinant AcpA, crystallization in presence of PEG 1500 with bound inhibitor vanadate resulting in three different crystal forms, X-ray diffraction structure determination and analysis of crystal form III at 1.75 A resolution |
