EC Number   |
|---|
   6.1.1.26 | 1.75 A X-ray crystal structure of the enzyme complexed with O-methyl-L-tyrosine and a non-hydrolyzable ATP analogue |
| 6.1.1.26 | apo-PylRS and PylRS complexes with different ligands, X-ray diffraction structure determination and analysis |
| 6.1.1.26 | crystal structure of PylRS apoenzyme and in complex with tRNAPy, to 2.5 and 3.1 A resolution, respectively. The protein forms a dimer in the crystal and in solution |
| 6.1.1.26 | crystal structures of a catalytic fragment of the enzyme complexed with N3-(tert-butyloxycarbonyl)-L-lysine and an ATP analog and with Nepsilon-allyloxycarbonyl-L-lysine reveals that the enzyme requires an Nepsilon-carbonyl group bearing a substituent with a certain size |
| 6.1.1.26 | crystal structures of the PylRS catalytic fragment in the substrate-free, ATP analogue (AMPPNP)-bound, and AMPPNP/pyrrolysine-bound forms, compared with other PylRS structures |
| 6.1.1.26 | efforts to crystalize full-length PylRS are not successful due to the low solubility of the protein. The N-terminal domain is highly insoluble and aggregates full-length PylRS. But using the truncated C-terminal catalytic core of PylRS from Methanosarcina mazei, apo-PylRS and PylRS complexes with different ligands are successfully determined |
| 6.1.1.26 | hanging-drop vapour-diffusion method at 21°C, the triclinic form crystals contain two PylRS dimers (four monomer molecules) in the asymmetric unit, in which the two subunits in one dimer each bind Nepsilon-(tert-butyloxycarbonyl)-L-lysyladenylate and the two subunits in the other dimer each bind AMP |
| 6.1.1.26 | mutant Y384F/A302T/N346V/C348W/V401L in complex with O-methyl-L-tyrosine, hanging drop vapor diffusion method, using |
| 6.1.1.26 | purified recombinant His-tagged N-terminally truncated enzyme form PylRS(c270) in complex with an ATP analogue AMP-PNP, hanging drop vapour diffusion method, in 100 mM sodium cacodylate, pH 6.8, containing 0.25 M NaCl, 5 mM MgSO4 and 5% w/v PEG 4000, 20°C, hexagonal crystals, X-ray diffraction structure determination and analysis at 1.9-2.6 A resolution |
| 6.1.1.26 | purified recombinant N-terminally His-tagged catalytic domain of PylRS complexed with either AMP-PNP, pyrrolysine-AMP plus pyrophosphate, or the pyrrolysine analogue N-epsilon-[(cylopentyloxy)carbonyl]-L-lysine plus ATP, vapour diffusion method, 10 mg/ml protein in 100 mM Tris, pH 7.0-8.0, 8-14% PEG 2000 monomethyl ether, 10 mM pyrrolysine, and10 mM AMP-PNP or other ligands, overnight at 16°C, stabilization and cryoprotection by 5 mM EDTA, 10 mM AMP-PNP, 5 mM MgCl2, 30% ethylen glycol, and additional 2% PEG, hexagonal-shaped crystals, X-ray diffraction structure determination and analysis at 1.8 A resolution |
