1OEC
FGFr2 kinase domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.6 |
Synchrotron site | SRS |
Beamline | PX9.6 |
Temperature [K] | 287 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 69.760, 80.500, 120.170 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 100.000 - 2.400 |
R-factor | 0.211 |
Rwork | 0.211 |
R-free | 0.28500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gjo |
RMSD bond length | 0.007 |
RMSD bond angle | 1.240 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.450 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.046 | 0.199 |
Number of reflections | 87022 | |
<I/σ(I)> | 22.1 | |
Completeness [%] | 98.0 | 78.9 |
Redundancy | 6.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.9 | pH 5.90 |