6V3R
Crystal structure of murine cycloxygenase in complex with a harmaline analog, 4,9-dihydro-3H-pyrido[3,4-b]indole
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 | 2016-04-13 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97918 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 217.154, 124.379, 136.539 |
Unit cell angles | 90.00, 123.84, 90.00 |
Refinement procedure
Resolution | 102.390 - 2.660 |
R-factor | 0.2207 |
Rwork | 0.219 |
R-free | 0.26380 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3nt1 |
RMSD bond length | 0.002 |
RMSD bond angle | 0.551 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 102.390 | 2.757 |
High resolution limit [Å] | 2.660 | 2.660 |
Rmerge | 0.157 | 1.076 |
Rmeas | 0.191 | |
Rpim | 0.106 | 0.738 |
Number of reflections | 85034 | 7373 |
<I/σ(I)> | 8.39 | 1.05 |
Completeness [%] | 98.0 | 85.82 |
Redundancy | 3.1 | 3 |
CC(1/2) | 0.988 | 0.521 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.7 | 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 |