8S1X
Crystal structure of Actinonin-bound PDF1 and the computationally designed DBAct553_1 protein binder
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-02-11 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.87313 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 49.440, 75.010, 83.160 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 55.700 - 1.880 |
| R-factor | 0.1846 |
| Rwork | 0.184 |
| R-free | 0.20270 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.779 |
| Data reduction software | autoPROC |
| Data scaling software | autoPROC |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.21_5184) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 55.700 | 1.910 |
| High resolution limit [Å] | 1.880 | 1.880 |
| Rmerge | 0.044 | 1.125 |
| Number of reflections | 24990 | 1266 |
| <I/σ(I)> | 15 | 1.3 |
| Completeness [%] | 96.9 | 99.6 |
| Redundancy | 4.3 | 4.4 |
| CC(1/2) | 0.999 | 0.426 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.2 | 291.15 | 0.2 M Sodium Formate, 0.1 M Sodium Phosphate pH 6.2, 20% (v/v) PEG smear, 10% (v/v) glycerol |
