44AC
Crystal structure of FGFR1 with a nucleoside scaffold-based inhibitor LJ5438
This is a non-PDB format compatible entry.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-1A |
| Synchrotron site | Photon Factory |
| Beamline | BL-1A |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2026-02-06 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 1.000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 211.880, 50.669, 65.336 |
| Unit cell angles | 90.00, 107.06, 90.00 |
Refinement procedure
| Resolution | 49.150 - 1.970 |
| R-factor | 0.2001 |
| Rwork | 0.199 |
| R-free | 0.22710 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.090 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX (2.0_5885) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.810 | 2.070 |
| High resolution limit [Å] | 1.970 | 1.970 |
| Number of reflections | 43719 | 14053 |
| <I/σ(I)> | 19.41 | |
| Completeness [%] | 92.8 | |
| Redundancy | 3.59 | |
| CC(1/2) | 0.999 | 0.959 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 295 | 0.2 M L-proline 0.1 M HEPES, pH 7.5 12% (w/v) PEG 3350 |
