5F1A
The Crystal Structure of Salicylate 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 | 2014-11-23 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.033 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 118.410, 132.660, 178.740 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 33.324 - 2.380 |
R-factor | 0.1759 |
Rwork | 0.174 |
R-free | 0.21810 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.922 |
Data reduction software | MOSFLM |
Data scaling software | Aimless (0.3.11) |
Phasing software | PHASER (2.5.6) |
Refinement software | PHENIX (1.9-1692) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 34.750 | 34.750 | 2.400 |
High resolution limit [Å] | 2.340 | 10.200 | 2.340 |
Rmerge | 0.112 | 0.034 | 0.720 |
Rpim | 0.061 | 0.019 | 0.403 |
Total number of observations | 241855 | 3096 | 17961 |
Number of reflections | 59216 | ||
<I/σ(I)> | 9.1 | 22.4 | 2.1 |
Completeness [%] | 99.5 | 97.4 | 99.4 |
Redundancy | 4.1 | 3.9 | 4 |
CC(1/2) | 0.994 | 0.998 | 0.701 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 296 | 22-34% PAA-5100, 100mM HEPES (pH 7.5), 20mM MgCl2, 0.6% BOG |