30TO
14-3-3sigma protein binding to TSC2-strong peptide (RSH mutation) and stabilizer 3'deAc FC-A.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-3 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-3 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-11-21 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.967697 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 82.147, 111.846, 62.706 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.569 - 1.800 |
| Rwork | 0.172 |
| R-free | 0.20930 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.124 |
| Data reduction software | autoPROC |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0431 (refmacat 0.4.126)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.570 | 1.840 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Number of reflections | 26916 | 1432 |
| <I/σ(I)> | 16.7 | 3.6 |
| Completeness [%] | 99.1 | |
| Redundancy | 14.8 | |
| CC(1/2) | 0.998 | 0.883 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277 | 0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400 |
