8XGK

Optimization Efforts for Identification of Novel Highly Potent Keap1-Nrf2 Protein-Protein Interaction Ihhibitors

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	103.251, 103.251, 55.186
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	46.960 - 1.320
R-factor	0.1627
Rwork	0.162
R-free	0.16860
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.017
RMSD bond angle	1.969
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]	89.420	1.340
High resolution limit [Å]	1.320	1.320
Rmerge	0.077	0.805
Rmeas	0.079
Rpim	0.017
Number of reflections	76523	3706
<I/σ(I)>	4.4
Completeness [%]	97.1
Redundancy	20.8
CC(1/2)	0.999

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