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