5IKV
The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-08-02 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1.00 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 126.918, 149.334, 184.766 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.009 - 2.508 |
R-factor | 0.1874 |
Rwork | 0.185 |
R-free | 0.22380 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 0.898 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.000 |
High resolution limit [Å] | 2.500 |
Number of reflections | 60238 |
<I/σ(I)> | 22.4 |
Completeness [%] | 100.0 |
Redundancy | 6.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 32% PEG 400, 100mM HEPES, 300mM Ammonium phosphate |