1OEC
FGFr2 kinase domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.6 |
| Synchrotron site | SRS |
| Beamline | PX9.6 |
| Temperature [K] | 287 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 69.760, 80.500, 120.170 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 100.000 - 2.400 |
| R-factor | 0.211 |
| Rwork | 0.211 |
| R-free | 0.28500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gjo |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.240 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.450 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.046 | 0.199 |
| Number of reflections | 87022 | |
| <I/σ(I)> | 22.1 | |
| Completeness [%] | 98.0 | 78.9 |
| Redundancy | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.9 | pH 5.90 |






