6V9C
Crystal structure of FGFR4 kinase domain in complex with covalent inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-06-20 |
| Detector | OXFORD SAPPHIRE CCD |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 44.067, 58.670, 60.747 |
| Unit cell angles | 90.00, 97.57, 90.00 |
Refinement procedure
| Resolution | 42.020 - 1.900 |
| R-factor | 0.201 |
| Rwork | 0.199 |
| R-free | 0.22700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3oxz |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.960 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | BUSTER (2.11.7) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.020 | 1.990 |
| High resolution limit [Å] | 1.900 | 1.940 |
| Rmerge | 0.049 | 0.560 |
| Number of reflections | 24253 | 1540 |
| <I/σ(I)> | 13.2 | |
| Completeness [%] | 98.6 | |
| Redundancy | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH MODE | 277 | 100 mM Bis-Tris pH 5.5, 14% (w/v) polyethylene glycol 3,350, 200 mM lithium sulfate and 2% (w/v) glycerol |
