6ZF0
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 | PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1) |
Synchrotron site | PETRA III, EMBL c/o DESY |
Beamline | P13 (MX1) |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-03-23 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.980201 |
Spacegroup name | P 61 |
Unit cell lengths | 103.304, 103.304, 55.951 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.440 - 1.600 |
R-factor | 0.1647 |
Rwork | 0.164 |
R-free | 0.18500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5fnu |
RMSD bond length | 0.008 |
RMSD bond angle | 1.072 |
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] | 47.440 | 1.656 |
High resolution limit [Å] | 1.599 | 1.599 |
Rmerge | 0.033 | 0.368 |
Rmeas | 0.041 | 0.460 |
Rpim | 0.024 | 0.272 |
Number of reflections | 42600 | 4135 |
<I/σ(I)> | 15.08 | 1.96 |
Completeness [%] | 94.5 | 91.91 |
Redundancy | 2.5 | 2.4 |
CC(1/2) | 0.999 | 0.855 |
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 |