9GFA
Crystal structure of 14-3-3 sigma in complex with Tau pS214 peptide and covalent stabilizer LD33
This is a non-PDB format compatible entry.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID30B |
| Synchrotron site | ESRF |
| Beamline | ID30B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-02-04 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.885601 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 82.384, 112.568, 62.459 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 66.480 - 1.600 |
| R-factor | 0.17466 |
| Rwork | 0.173 |
| R-free | 0.19621 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.570 |
| Data reduction software | autoPROC |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 66.480 | 1.630 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Number of reflections | 38694 | 1894 |
| <I/σ(I)> | 22.6 | |
| Completeness [%] | 100.0 | |
| Redundancy | 11.7 | |
| CC(1/2) | 0.999 | 0.954 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277 | 10mg/mL 14-3-3sigma delta C, 1.5eq peptide, 0.095 M HEPES pH 7.1, 28% PEG400, 0.19 M CaCl2, 5% (v/v) glycerol compound soaked |
