6P68
Crystal structure of FGFR1-Y563C (FGFR4 surrogate) covalently bound to compound 22.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 120 |
| Detector technology | CCD |
| Collection date | 2014-08-14 |
| Detector | RAYONIX MX300-HS |
| Wavelength(s) | 1.000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 192.500, 79.273, 96.718 |
| Unit cell angles | 90.00, 110.53, 90.00 |
Refinement procedure
| Resolution | 48.280 - 2.900 |
| R-factor | 0.22951 |
| Rwork | 0.226 |
| R-free | 0.30265 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3rhx |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.516 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.000 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.062 | 0.290 |
| Number of reflections | 28812 | 1973 |
| <I/σ(I)> | 19.3 | 2.7 |
| Completeness [%] | 94.2 | |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | 1:1 mix of protein + reservoir Protein at ~15 mg/mL formulated in: 20mM Tris pH 8, 20mM NaCl, 2mM TCEP Reservoir: 14-18% PEG 10K 0.3 M (NH4)2SO4 0.1 M MES pH 6.5 5% ethylene glycol |
