EC Number   |
|---|
   2.7.1.107 | Ca2+-bound EF-hand domain of isoform DGKalpha, sitting drop vapor diffusion method, using 0.1 M HEPES, pH 7.0, 1.0 M succinic acid, and 1% (w/v) PEG monomethyl ether 2000 |
| 2.7.1.107 | isoform DgkB, both as free enzyme and in complex with ADP, 2.4 and 2.3 A resolution, respectively. Enzyme is a tight homodimer, and each monomer comprises two domains with the catalytic center located within the interdomain cleft |
| 2.7.1.107 | purified kinase captured as a ternary complex with bound lipid substrate and an ATP analogue, method optimization, microseeding, the precipitant solution contains 0.2% v/v MPD, 0.1 M NaCl, 0.05 M Na3C6H5O7, pH 5.6, 20°C, X-ray diffraction structure determination and analysis at resolutions of 2.18-3.20 A |
| 2.7.1.107 | purified recombinanz wild-type and DELTA4 and DELTA7 mutant enzymes in complex with lipid substrate and ATP, 20°C, X-ray diffraction structure determination and analysis at 2.05 A resolution, structure mmodeling. The kinase adopts a functional form in the crystal. Domain swapping, a key feature of the solution form, is not observed in the crystal structures. Crystals of mutant DELTA7 DgkA are soaked with the ATP analogue, adenylylmethylenediphosphate (Mg2+-AMPPCP). This causes the crystals to dissolve. Additional soaking with ATP, ADP, AMP, ATP?S, AMPPNP and dATP but not with GTP, CTP, UTP or TTP leads to crystal dissolution |
| 2.7.1.107 | sitting-drop vapour-diffusion method. Crystals belong to space group P2(1), with unit-cell parameters a = 42.4, b = 166.1, c = 48.5 A, beta = 96.97° |
