9GGA
Crystal structure of 14-3-3 sigma in complex with Tau pS214 peptide and covalent stabilizer FM089
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 EIGER2 X 9M |
| Wavelength(s) | 0.885601 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 82.516, 112.340, 62.729 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 56.170 - 2.240 |
| R-factor | 0.1944 |
| Rwork | 0.194 |
| R-free | 0.19920 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.427 |
| 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] | 66.500 | 2.310 |
| High resolution limit [Å] | 2.240 | 2.240 |
| Number of reflections | 72024 | 6515 |
| <I/σ(I)> | 18.5 | |
| Completeness [%] | 99.3 | |
| Redundancy | 5.1 | |
| CC(1/2) | 0.995 | 0.838 |
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 |
