5F28
Crystal structure of FAT domain of Focal Adhesion Kinase (FAK) bound to the transcription factor MEF2C
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-04-11 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.8729 |
| Spacegroup name | P 42 21 2 |
| Unit cell lengths | 139.210, 139.210, 90.350 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.221 - 2.900 |
| R-factor | 0.2097 |
| Rwork | 0.208 |
| R-free | 0.23540 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB entries 1K40 (FAT) and 3KOV (MEF2) |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.593 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((dev_2196)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.220 | 3.080 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.344 | 1.559 |
| Number of reflections | 37566 | |
| <I/σ(I)> | 8.7 | 1.9 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 13.7 | 13.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | 0.1M Magnseium acetate, 0.1M MES, pH 6.5, 12% PEG 8000 |






