9R2O
De novo designed N5 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) | 0.965459 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 112.710, 38.250, 77.470 |
| Unit cell angles | 90.00, 112.64, 90.00 |
Refinement procedure
| Resolution | 52.830 - 2.090 |
| R-factor | 0.2437 |
| Rwork | 0.242 |
| R-free | 0.27190 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.422 |
| 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] | 52.833 | 2.121 |
| High resolution limit [Å] | 2.085 | 2.085 |
| Rmerge | 0.106 | 0.759 |
| Number of reflections | 18349 | 947 |
| <I/σ(I)> | 8.4 | 1.6 |
| Completeness [%] | 98.9 | 99.4 |
| Redundancy | 3.2 | 3.2 |
| CC(1/2) | 0.996 | 0.343 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 291.15 | 0.1 M MES 6.5, 25% w/v PEG 2000 MME, 0.2 M KSCN |
