3RI1
Crystal structure of the catalytic domain of FGFR2 kinase in complex with ARQ 069
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-10-17 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.075 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 105.794, 119.581, 63.311 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.100 |
R-factor | 0.21597 |
Rwork | 0.214 |
R-free | 0.24746 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.008 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.100 |
Number of reflections | 46498 |
Completeness [%] | 97.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 15% polyethylene glycol 4000 and 0.3M lithium sulfate and 100 mM HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |