8RBH
Crystal structure of the kelch domain of human KLHL12 in complex with PEF1 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04 |
Synchrotron site | Diamond |
Beamline | I04 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-03-08 |
Detector | DECTRIS EIGER2 XE 16M |
Wavelength(s) | 0.976254 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.001, 78.390, 73.784 |
Unit cell angles | 90.00, 99.24, 90.00 |
Refinement procedure
Resolution | 72.830 - 1.880 |
R-factor | 0.212 |
Rwork | 0.210 |
R-free | 0.25760 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.010 |
Data reduction software | xia2 |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 72.830 | 1.910 |
High resolution limit [Å] | 1.880 | 1.880 |
Rmerge | 0.283 | 3.843 |
Rmeas | 0.306 | 4.154 |
Rpim | 0.115 | 1.562 |
Number of reflections | 40172 | 1936 |
<I/σ(I)> | 6.2 | 0.6 |
Completeness [%] | 97.6 | 94.58 |
Redundancy | 6.928 | |
CC(1/2) | 0.992 | 0.189 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293.15 | 0.1 M BIS-TRIS pH 5.5, 200 mM NaCl, and 30% PEG4K. (1:1) |