5UHN
Crystal Structure of the Tyrosine Kinase Domain of FGF Receptor 2 harboring a N549H/E565A Double Gain-of-Function Mutation
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 | 2012-09-24 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.97885 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 67.334, 78.557, 116.546 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.279 - 2.909 |
R-factor | 0.2597 |
Rwork | 0.254 |
R-free | 0.31120 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2psq |
RMSD bond length | 0.002 |
RMSD bond angle | 0.467 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.950 |
High resolution limit [Å] | 2.900 | 2.900 |
Number of reflections | 14079 | |
<I/σ(I)> | 26.5 | 7.2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 14 | 12.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 25 mM HEPES (pH 7.5), 15-25% w/v PEG 4000, 0.2-0.3 M Ammonium Sulfate |