6FR2

Soluble epoxide hydrolase in complex with LK864

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID29
Synchrotron site	ESRF
Beamline	ID29
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-09-16
Detector	DECTRIS PILATUS 6M
Wavelength(s)	1.072
Spacegroup name	I 2 2 2
Unit cell lengths	80.091, 92.180, 106.998
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.090 - 2.262
R-factor	0.1698
Rwork	0.168
R-free	0.21000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4jnc
RMSD bond length	0.011
RMSD bond angle	0.955
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	PHENIX (1.12_2829)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	46.090	46.090	2.300
High resolution limit [Å]	2.260	20.000	2.260
Rmerge	0.081	0.052	0.788
Rmeas	0.096	0.062	0.955
Total number of observations	120149
Number of reflections	35335	48	1497
<I/σ(I)>	9.4	21.89	1.71
Completeness [%]	98.5	88.9	82.7
Redundancy	3.4	3.021	2.983
CC(1/2)	0.996	0.995	0.779

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		277	1 uL protein solution Protein (5-10 mg/mL , 50 mM NaCl, 50 mM sodium phosphate, 10% glycerol (98%), 2 mM DTT at pH 7.4) was mixed in different ratios (2/1, 1/1, 1/2) with precipitant solution (23 %-28 % (w/v) polyethylenglycol (PEG) 6000, 70 mM ammonium acetat, 200 mM magnesium acetat, 100 mM sodium cacodylate at pH 6.1-6.5)