5WG1
Kelch domain of human Keap1 bound to mutant Nrf2 EAGE peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-01-22 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.97946 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 161.809, 68.649, 77.126 |
Unit cell angles | 90.00, 117.54, 90.00 |
Refinement procedure
Resolution | 34.325 - 2.021 |
R-factor | 0.2334 |
Rwork | 0.232 |
R-free | 0.26760 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5wfl |
RMSD bond length | 0.004 |
RMSD bond angle | 0.688 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 34.320 | 2.094 |
High resolution limit [Å] | 2.021 | 2.021 |
Rmerge | 0.154 | 0.327 |
Number of reflections | 46561 | 4570 |
<I/σ(I)> | 6.27 | 2.03 |
Completeness [%] | 95.0 | 94 |
Redundancy | 2.5 | 2.5 |
CC(1/2) | 0.971 | 0.862 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 290 | 1.2 - 1.5 M Ammonium sulfate, 0.1 M Bis-Tris pH = 6.0 - 6.5 |