8I2A
E. coli tryptophanyl-tRNA synthetase bound with a chemical fragment at the dimerization interface
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-11-19 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9785 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.741, 80.539, 77.258 |
| Unit cell angles | 90.00, 106.30, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.350 |
| R-factor | 0.21578 |
| Rwork | 0.214 |
| R-free | 0.24408 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5v0i |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.102 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.440 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.126 | 0.614 |
| Rmeas | 0.151 | 0.732 |
| Rpim | 0.081 | 0.395 |
| Total number of observations | 10471 | |
| Number of reflections | 30223 | 3155 |
| <I/σ(I)> | 7 | 2 |
| Completeness [%] | 99.5 | |
| Redundancy | 3.4 | 3.3 |
| CC(1/2) | 0.990 | 0.744 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 290 | 0.16M Ammonium sulfate, 0.1M HEPES pH 7.5, 25% PEG 3350 |
