8XGV

Optimization Efforts for Identification of Novel Highly Potent Keap1-Nrf2 Protein-Protein Interaction (PPI) Inhibitors

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE BL-17A
Synchrotron site	Photon Factory
Beamline	BL-17A
Temperature [K]	100
Detector technology	PIXEL
Collection date	2015-06-02
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.9800
Spacegroup name	P 61
Unit cell lengths	103.581, 103.581, 55.469
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	47.180 - 1.420
R-factor	0.1672
Rwork	0.167
R-free	0.16890
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.258
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.20_4459)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	55.470	1.430
High resolution limit [Å]	1.410	1.410
Rmerge	0.077
Rmeas	0.079
Rpim	0.017
Number of reflections	64842	3197
<I/σ(I)>	27.5
Completeness [%]	99.1
Redundancy	20.3
CC(1/2)	0.999	0.938

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	5	277	The purified Keap1 Kelch domain was concentrated to 6-10 mg/mL and crystallized with the solution containing 0.1 M Na acetate (pH 5.0) and 1.5 M di-ammonium sulfate, and 0-0.15 M NaCl