EC Number   |
|---|
   3.5.3.15 | - |
| 3.5.3.15 | 27 structures and calcium-titrations by X-ray crystallography to determine order of binding and affinity for the six calcium ions that bind and activate the enzyme |
| 3.5.3.15 | Ca2+-free enzyme |
| 3.5.3.15 | crystal structures of a Ca2+-bound PAD4 mutant C645A in complex with three histone N-terminal peptides, each consisting of 10 amino acid residues that include one target arginine residue for the enzyme (H3/Arg-8, H3/Arg-17, and H4/Arg-3). hanging-drop vapor-diffusion method |
| 3.5.3.15 | hanging drop vapor diffusion method, using 0.2 M CaCl2, 20% (w/v) polyethylene glycol 3350 |
| 3.5.3.15 | hanging drop vapor diffusion method, using 20 mM imidazole buffer pH 7.0, 0.2 M Li2SO4, 15% (w/v) polyethylene glycol monomethylether 5000 |
| 3.5.3.15 | in complex with inhibitor Cl-amidine, to 1.6 A resolution |
| 3.5.3.15 | purified recombinant GST-tagged PAD4 mutant C645A in complex with Ca2+ and histone-derived N-terminal peptide substrates, hanging-drop vapor-diffusion method, soaking of Ca2+-free crystals in crystallization buffer containing 5 mM CaCl2 and each histone N-terminal peptide for 8 h at 20°C, X-ray diffraction structure determination and anaylsis at 2.0-2.225 A resolution, molecular replacement |
| 3.5.3.15 | sitting-drop vapor-diffusion technique at 23°C, apoPAD2 crystals with increasing concentrations of calcium (0-10 mM), 16 structures are solved at eight different calcium concentrations to 1.66-1.97 A |
| 3.5.3.15 | structure of isoform Pad1, in presence of Ca2+, to 3.2 A resolution. The asymmetric unit containes two PAD1 molecules, with an elongated N-terminal loop that appears to prevent the formation of a homodimer. The N-terminal loop occupies the substrate binding site of the adjacent PAD1 molecules in the crystal |
