1GJO
The FGFr2 tyrosine kinase domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.5 |
| Synchrotron site | SRS |
| Beamline | PX9.5 |
| Temperature [K] | 291 |
| Detector technology | CCD |
| Detector | MARRESEARCH |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 69.758, 80.983, 120.059 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.400 |
| R-factor | 0.214 |
| Rwork | 0.214 |
| R-free | 0.25600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fgk |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.268 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | X-PLOR (98) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.039 | 0.163 |
| Number of reflections | 75710 | |
| <I/σ(I)> | 10.8 | |
| Completeness [%] | 98.6 | 97.1 |
| Redundancy | 5.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.9 | 32% AMMONIUM SULFATE, TRIS/MALEIC ACID BUFFER, PH 5.9 |
