8VSL
Binary structure of 14-3-3 sigma and ARAF phosphopeptide (pS214)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2023-05-15 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 0.967697 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 82.518, 112.806, 62.713 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 66.600 - 1.420 |
R-factor | 0.1836 |
Rwork | 0.182 |
R-free | 0.20798 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.807 |
Data reduction software | autoPROC |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | PDB-REDO |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 66.600 | 1.440 |
High resolution limit [Å] | 1.420 | 1.420 |
Number of reflections | 55423 | 2702 |
<I/σ(I)> | 11.8 | 1.5 |
Completeness [%] | 99.9 | |
Redundancy | 13.4 | |
CC(1/2) | 0.997 | 0.536 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 277.15 | PEG400, HEPES, CaCl2, glycerol |