5EG3
Crystal Structure of the Activated FGF Receptor 2 (FGFR2) Kinase Domain in complex with the cSH2 domain of Phospholipase C gamma (PLCgamma)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4C |
| Synchrotron site | NSLS |
| Beamline | X4C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-07-20 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.97907 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 79.609, 53.231, 127.660 |
| Unit cell angles | 90.00, 100.11, 90.00 |
Refinement procedure
| Resolution | 37.859 - 2.606 |
| R-factor | 0.1907 |
| Rwork | 0.185 |
| R-free | 0.23730 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2pvy 2ple |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.210 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.859 | 2.640 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.256 | |
| Number of reflections | 15981 | |
| <I/σ(I)> | 27.9 | 5.9 |
| Completeness [%] | 98.2 | 93.5 |
| Redundancy | 6.6 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 25 mM HEPES (pH 7.5), PEG20000 (12% 18%) and 2% (w/v) Benzamidine hydrochloride |
