9FS4
Crystal structure of 14-3-3 sigma in complex with Tau pS214 peptide and covalent stabilizer LD12
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-12-01 |
| Detector | DECTRIS EIGER2 X 16M |
| Wavelength(s) | 0.972425 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 82.343, 112.226, 62.420 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 66.390 - 1.600 |
| R-factor | 0.18256 |
| Rwork | 0.182 |
| R-free | 0.19776 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.894 |
| Data reduction software | autoPROC |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (Refmac5) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 66.390 | 1.630 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Number of reflections | 35088 | 1884 |
| <I/σ(I)> | 27.4 | |
| Completeness [%] | 91.1 | |
| Redundancy | 1.9 | |
| CC(1/2) | 1.000 | 0.967 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING 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 |
