9R2V
De novo designed M16 protein fold
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 | 2024-09-21 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.91840 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.250, 82.110, 111.420 |
| Unit cell angles | 90.00, 92.45, 90.00 |
Refinement procedure
| Resolution | 61.190 - 2.490 |
| R-factor | 0.2374 |
| Rwork | 0.234 |
| R-free | 0.29040 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.449 |
| Data reduction software | autoPROC |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.21.2_5419) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 111.318 | 2.535 |
| High resolution limit [Å] | 2.490 | 2.492 |
| Rmerge | 0.038 | 0.677 |
| Number of reflections | 35326 | 1724 |
| <I/σ(I)> | 12.8 | 1.3 |
| Completeness [%] | 91.2 | 89.6 |
| Redundancy | 2.5 | |
| CC(1/2) | 0.999 | 0.554 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 291.15 | 0.04 M Calcium chloride dihydrate 0.04 M Sodium formate 0.1 M Tris 8.0 25 % v/v PEG Smear Low |
