9R2R
De novo designed M7 protein fold
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 | 2025-02-17 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.96546 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 101.480, 88.580, 65.750 |
| Unit cell angles | 90.00, 114.04, 90.00 |
Refinement procedure
| Resolution | 60.050 - 2.910 |
| R-factor | 0.2508 |
| Rwork | 0.248 |
| R-free | 0.30220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.417 |
| 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] | 60.050 | 2.965 |
| High resolution limit [Å] | 2.910 | 2.910 |
| Rmerge | 0.088 | 1.028 |
| Number of reflections | 10973 | 562 |
| <I/σ(I)> | 9.5 | 1.3 |
| Completeness [%] | 93.8 | 99.8 |
| Redundancy | 3.3 | 3.5 |
| CC(1/2) | 0.999 | 0.495 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 291.15 | 0.1 M MES 6.5, 0.2 M KSCN, 15% w/v PEG 4000 |
