7OFF

Keap1 kelch domain bound to a small molecule inhibitor of the Keap1-Nrf2 protein-protein interaction

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX IV BEAMLINE BioMAX
Synchrotron site	MAX IV
Beamline	BioMAX
Temperature [K]	100
Detector technology	PIXEL
Collection date	2019-12-01
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.9763
Spacegroup name	P 61
Unit cell lengths	103.190, 103.190, 55.600
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	51.590 - 1.370
R-factor	0.151
Rwork	0.150
R-free	0.17300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5fnu
RMSD bond length	0.007
RMSD bond angle	1.006
Data reduction software	XDS (v Mar 15, 2019)
Data scaling software	XDS (v Mar 15, 2019)
Phasing software	PHASER (1.13_2998)
Refinement software	PHENIX (1.13_2998)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	51.590	1.416
High resolution limit [Å]	1.367	1.367
Rmerge	0.096	1.328
Rmeas	0.098	1.400
Rpim	0.022	0.434
Number of reflections	71319	7092
<I/σ(I)>	21.56	2.09
Completeness [%]	100.0	99.9
Redundancy	17.9	9.9
CC(1/2)	1.000	0.847

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6	293	0.5 M Ammonium sulfate, 0.1 M Sodium citrate tribasic dihydrate pH 5.6 and 1.0 M Lithium sulfate monohydrate