8XLO
FGFR1 kinase domain with a dual-warhead covalent inhibitor CXF-007
This is a non-PDB format compatible entry.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 80 |
| Detector technology | CCD |
| Collection date | 2020-05-31 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97918 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 209.210, 57.480, 66.410 |
| Unit cell angles | 90.00, 107.86, 90.00 |
Refinement procedure
| Resolution | 46.683 - 2.360 |
| R-factor | 0.2101 |
| Rwork | 0.208 |
| R-free | 0.25450 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7wcl |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.647 |
| Data reduction software | DIALS |
| Data scaling software | EVAL15 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.683 | 2.444 |
| High resolution limit [Å] | 2.360 | 2.360 |
| Rmerge | 0.071 | 1.112 |
| Rmeas | 0.077 | 1.201 |
| Number of reflections | 31130 | 3091 |
| <I/σ(I)> | 14.79 | 2.12 |
| Completeness [%] | 99.6 | 99.87 |
| Redundancy | 6.7 | 7.1 |
| CC(1/2) | 0.999 | 0.801 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277.15 | 18% (w/v) PEG 8000, 0.2 M Li2SO4, and 0.1 M MES, pH 6.5 |
