3DAR
Crystal structure of D2 domain from human FGFR2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-05-06 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9763 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 41.870, 78.240, 85.900 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.917 - 2.200 |
| R-factor | 0.2188 |
| Rwork | 0.212 |
| R-free | 0.25500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PBD Entry 1E0O chain B residues 149-249 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.149 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.2.25) |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 85.900 | 33.920 | 2.320 |
| High resolution limit [Å] | 2.200 | 6.960 | 2.200 |
| Rmerge | 0.080 | 0.031 | 0.623 |
| Total number of observations | 3509 | 15291 | |
| Number of reflections | 14667 | ||
| <I/σ(I)> | 6.7 | 16.3 | 1.2 |
| Completeness [%] | 98.8 | 97.5 | 98.1 |
| Redundancy | 7.3 | 6.7 | 7.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | 0.2 M sodium acetate, 0.1 M Tris-HCl, 30% PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K, pH 8.5 |






