8Q1R
mouse Keap1 in complex with stapled peptide
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 | 2023-03-29 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.976254 |
Spacegroup name | P 61 |
Unit cell lengths | 103.039, 103.039, 55.727 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.220 - 1.330 |
R-factor | 0.1973 |
Rwork | 0.196 |
R-free | 0.22870 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.012 |
RMSD bond angle | 1.210 |
Data reduction software | autoPROC |
Data scaling software | autoPROC |
Phasing software | PHASER |
Refinement software | BUSTER (2.11.8 (8-JUN-2022)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 89.234 | 1.430 |
High resolution limit [Å] | 1.330 | 1.330 |
Rmerge | 0.082 | 0.762 |
Number of reflections | 523089 | 2656 |
<I/σ(I)> | 12.3 | |
Completeness [%] | 88.3 | |
Redundancy | 9.8 | |
CC(1/2) | 0.998 | 0.571 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 5.9 | 293 | 0.7-0.9M Lithium Sulfate, 0.5-0.7M Ammonium sulfate and 0.1M Sodium Citrate pH5.9 |