3RHX
Crystal structure of the catalytic domain of FGFR1 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 | 2009-09-03 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.075 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 208.430, 57.865, 65.686 |
Unit cell angles | 90.00, 107.22, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.010 |
R-factor | 0.20456 |
Rwork | 0.201 |
R-free | 0.26167 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.022 |
RMSD bond angle | 1.854 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.010 |
Number of reflections | 59198 |
Completeness [%] | 97.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | PEG 10000, 0.3M (NH4)2SO4, 5% ethylene glycol, 100mM MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |