4OTY

Crystal structure of lumiracoxib bound to the apo-mouse-cyclooxygenase-2

Replaces:  4LLZ

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