EC Number   |
|---|
   1.14.11.69 | catalytic core of Rph1, hanging drop vapour diffusion method, X-ray diffraction structure determination and analysis at 2.5 A resolution |
| 1.14.11.69 | crystal structure determinations of JMJD2A in complex with histone H3 peptides bearing different methylated forms of K9 and K36 |
| 1.14.11.69 | purified JMJD2A catalytic domain in complex with H3K9me3, H3K36me2 and H3K36me3 peptides, vapor diffusion method, from 0.2 M sodium/potassium phosphate, pH 6.5, and 20% w/v PEG 3350, at 4°C, and by microseeding from 12% w/v PEG monomethyl ether 5000 and 0.1 M HEPES, pH 7.0, X-ray diffraction structure determination and analysis at 2.05-2.30 A resolution |
| 1.14.11.69 | purified recombinant enzyme in complex with inhibitor, sitting drop vapor diffusion method, mixing of 7 mg/ml protein and 2 mM N-oxalylglycine with well solution, containing 25% v/v PEG 3350, 0.2 M sodium nitrate, 0.1 M bis-tris propane, pH 6.5, 5% v/v ethylene glycol, 0.01 M NiCl2, in a 2:1 ratio, 4°C, X-ray diffraction structure determination and analysis at 2.55 A resolution |
| 1.14.11.69 | purified recombinant enzyme in complex with substrate peptides, by vapour diffusion at 4°C from 0.1 M citrate, pH 5.5, 20% PEG 3350 and 4 mM NiCl2, X-ray diffraction structure determination and analysis at 2.1 A resolution |
| 1.14.11.69 | purified recombinant JMJD2A catalytic core complexed with methylated H3K36 peptide substrates (trimethylated H3K36 peptide (H3K36me3) or a monomethylated H3K36 peptide (H3K36me)) in the presence of Fe(II) and N-oxalylglycine, vapor diffusion method at 4°C against a solution containing 200 mM MgCl2, 100 mM Tris, pH 8.5, and 13-15% PEG 5000, X-ray diffraction structure determination and analysis at 2.0 A resolution |
| 1.14.11.69 | structures of the JMJD2A catalytic domain in complex with H3K9me3, H3K36me2 and H3K36me3 peptides. The histone substrates are recognized through a network of backbone hydrogen bonds and hydrophobic interactions that deposit the trimethyllysine into the active site. The trimethylated epsilon-ammonium cation is coordinated within a methylammonium-binding pocket through carbonoxygen hydrogen bonds that position one of the theta-methyl groups adjacent to the Fe(II) center for hydroxylation and demethylation |
