9O68
Crystal Structure of Tryptophanyl-tRNA synthetase from Klebsiella aerogenes (tryptophan bound)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS-II BEAMLINE 19-ID |
| Synchrotron site | NSLS-II |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-12-15 |
| Detector | DECTRIS EIGER2 XE 9M |
| Wavelength(s) | 0.9786 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 49.054, 120.798, 55.830 |
| Unit cell angles | 90.00, 94.87, 90.00 |
Refinement procedure
| Resolution | 48.880 - 2.150 |
| R-factor | 0.1821 |
| Rwork | 0.180 |
| R-free | 0.22250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.566 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (dev_5660) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.880 | 2.220 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.058 | 0.551 |
| Rmeas | 0.069 | 0.657 |
| Rpim | 0.037 | 0.353 |
| Total number of observations | 120058 | 9365 |
| Number of reflections | 34439 | 2868 |
| <I/σ(I)> | 12.6 | 2.2 |
| Completeness [%] | 98.0 | |
| Redundancy | 3.5 | 3.3 |
| CC(1/2) | 0.999 | 0.769 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | Berkeley |
