4ZSA
Crystal structure of FGFR1 kinase domain in complex with 7n
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-09-03 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9791 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 209.910, 57.181, 65.550 |
| Unit cell angles | 90.00, 107.47, 90.00 |
Refinement procedure
| Resolution | 34.366 - 2.000 |
| R-factor | 0.2056 |
| Rwork | 0.204 |
| R-free | 0.25410 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1agw |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.143 |
| Data reduction software | Coot |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER (2.5.3) |
| Refinement software | PHENIX (1.9_1692) |
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 | 0.055 | 0.028 | 0.486 |
| Rmeas | 0.065 | 0.033 | 0.566 |
| Rpim | 0.033 | 0.017 | 0.290 |
| Total number of observations | 187569 | ||
| Number of reflections | 50138 | ||
| <I/σ(I)> | 15.4 | ||
| Completeness [%] | 99.5 | 92.6 | 99.8 |
| Redundancy | 3.7 | 3.6 | 3.7 |
| CC(1/2) | 0.998 | 0.896 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | 0.1M Bis-Tris pH 6.5, 0.3M (NH4)2SO4, 15-20% PEG10000, 5% EG |
