9R2L
De novo designed N37 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 | 2024-11-14 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.87313 |
| Spacegroup name | P 1 |
| Unit cell lengths | 62.760, 66.840, 81.120 |
| Unit cell angles | 78.81, 74.75, 62.56 |
Refinement procedure
| Resolution | 77.980 - 2.200 |
| R-factor | 0.2009 |
| Rwork | 0.199 |
| R-free | 0.23180 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.387 |
| 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] | 77.980 | 2.237 |
| High resolution limit [Å] | 2.199 | 2.199 |
| Rmerge | 0.137 | 1.042 |
| Number of reflections | 56016 | 2788 |
| <I/σ(I)> | 7.3 | 1.3 |
| Completeness [%] | 98.0 | 97.2 |
| Redundancy | 4 | 4.1 |
| CC(1/2) | 0.995 | 0.551 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 291.15 | 0.2 M Potassium thiocyanate 0.1 M Sodium acetate 5.5 25 % w/v PEG 2000 MME |
