7WCL
Crystal structure of FGFR1 kinase domain with Pemigatinib
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | Cu FINE FOCUS |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2021-08-01 |
| Detector | RIGAKU |
| Wavelength(s) | 1.5870 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 210.831, 49.594, 66.804 |
| Unit cell angles | 90.00, 107.50, 90.00 |
Refinement procedure
| Resolution | 39.866 - 2.495 |
| R-factor | 0.1949 |
| Rwork | 0.193 |
| R-free | 0.23010 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4rwj |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.694 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.870 | 2.584 |
| High resolution limit [Å] | 2.495 | 2.495 |
| Rmerge | 0.070 | 0.288 |
| Rmeas | 0.079 | |
| Number of reflections | 21761 | 1416 |
| <I/σ(I)> | 15.13 | 3.05 |
| Completeness [%] | 93.5 | 61.78 |
| Redundancy | 4.5 | 3 |
| CC(1/2) | 0.998 | 0.922 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277.15 | 18% (w/v) PEG 8000, 0.2 M LiSO4, 0.1 M MES (pH 6.5) |
