Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-10-05 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97918 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 122.663, 133.173, 181.546 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.121 - 2.354 |
| R-factor | 0.1811 |
| Rwork | 0.180 |
| R-free | 0.22140 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3nt1 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.815 |
| Data reduction software | XDS |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.430 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.073 | 0.493 |
| Number of reflections | 61543 | |
| <I/σ(I)> | 6.7 | 6.7 |
| Completeness [%] | 99.6 | 98 |
| Redundancy | 5.8 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291 | mCOX-2 protein reconstituted with a 2-fold molar excess of heme in phosphtate buffer, pH 6.7, 100 mM NaCl, 1.2% (w/v) -OG, and 0.1% NaN3, and 10-fold molar excess of inhibitors from 25 mM DMSO stocks were added to protein samples. Mixing 3 uL of the protein-inhibitor complex with 3 uL crystallization solution containing 50 mM EPPS, pH 8.0, 120 mM MgCl2, 22-26% PEG MME-550 against reservoir solutions comprised of 50 mM EPPS pH 8.0, 120 mM MgCl2, 22-26% PEG MME-550, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
