9LOT
Crystal structure of Escherichia coli trptophanyl-tRNA synthetase in complex with N-piperidine ibrutinib
This is a non-PDB format compatible entry.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL02U1 |
| Synchrotron site | SSRF |
| Beamline | BL02U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-10-20 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.768, 79.649, 78.361 |
| Unit cell angles | 90.00, 105.78, 90.00 |
Refinement procedure
| Resolution | 54.490 - 1.590 |
| R-factor | 0.18985 |
| Rwork | 0.189 |
| R-free | 0.20487 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 8i1y |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.286 |
| Data reduction software | autoPROC |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 75.410 | 1.670 |
| High resolution limit [Å] | 1.590 | 1.590 |
| Rmerge | 0.094 | 1.535 |
| Number of reflections | 98739 | 14351 |
| <I/σ(I)> | 9 | 1.4 |
| Completeness [%] | 99.9 | |
| Redundancy | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 290 | 0.15 M ammonium sulfate, 0.1M HEPES pH 7.5, 25% w/v PEG 3,350 |
