8I2J
E. coli tryptophanyl-tRNA synthetase bound with a chemical fragment at the dimerization interface
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 110 |
| Detector technology | PIXEL |
| Collection date | 2022-05-01 |
| Detector | RIGAKU HyPix-6000HE |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.795, 80.423, 78.658 |
| Unit cell angles | 90.00, 105.65, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.650 |
| R-factor | 0.22624 |
| Rwork | 0.224 |
| R-free | 0.26021 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5v0i |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.048 |
| Data reduction software | CrysalisPro |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.790 |
| High resolution limit [Å] | 2.650 | 2.650 |
| Rmeas | 0.164 | 0.467 |
| Rpim | 0.079 | 0.225 |
| Total number of observations | 13122 | |
| Number of reflections | 21631 | 3166 |
| <I/σ(I)> | 9.6 | 3.6 |
| Completeness [%] | 99.7 | |
| Redundancy | 4 | 4.1 |
| CC(1/2) | 0.984 | 0.853 |
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 |
