6ITJ
Crystal structure of FGFR1 kinase domain in complex with compound 3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-07-16 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 0.979 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 209.628, 58.603, 65.709 |
| Unit cell angles | 90.00, 107.49, 90.00 |
Refinement procedure
| Resolution | 40.202 - 1.994 |
| R-factor | 0.2014 |
| Rwork | 0.199 |
| R-free | 0.24370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4zsa |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.935 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER (2.5.6) |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.030 |
| High resolution limit [Å] | 2.000 | 5.430 | 2.000 |
| Rmerge | 0.076 | 0.039 | 0.660 |
| Rmeas | 0.091 | 0.047 | 0.781 |
| Rpim | 0.049 | 0.025 | 0.415 |
| Total number of observations | 175256 | ||
| Number of reflections | 51283 | 2690 | 2532 |
| <I/σ(I)> | 6 | ||
| Completeness [%] | 98.7 | 99.2 | 97.6 |
| Redundancy | 3.4 | 3.3 | 3.5 |
| CC(1/2) | 0.995 | 0.819 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 277 | 0.1M Bis-Tris pH 6.5, 0.3M (NH4)2SO4, 15-20% PEG10000, 5% EG |
