8KH6
Crystal structure of FGFR4 kinase domain with 8r
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U1 |
| Synchrotron site | SSRF |
| Beamline | BL17U1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2023-01-02 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 41.780, 61.180, 60.720 |
| Unit cell angles | 90.00, 97.76, 90.00 |
Refinement procedure
| Resolution | 27.270 - 1.620 |
| R-factor | 0.205 |
| Rwork | 0.204 |
| R-free | 0.22760 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7ybo |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.966 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.19.2_4158: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 27.270 | 7.240 |
| High resolution limit [Å] | 1.620 | 1.620 |
| Number of reflections | 37228 | 37169 |
| <I/σ(I)> | 14.8 | |
| Completeness [%] | 96.2 | |
| Redundancy | 6.2 | |
| CC(1/2) | 0.999 | 0.999 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277 | 0.1 M Bis-Tris (pH 4.5), 0.2 M Li2SO4, 16-19% PEG 3350 |






