9R2K
De novo designed N30 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 | 2024-06-27 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.96546 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 75.600, 39.810, 54.630 |
| Unit cell angles | 90.00, 99.35, 90.00 |
Refinement procedure
| Resolution | 53.900 - 1.960 |
| R-factor | 0.1995 |
| Rwork | 0.197 |
| R-free | 0.25250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.855 |
| 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] | 53.904 | 1.995 |
| High resolution limit [Å] | 1.960 | 1.961 |
| Rmerge | 0.161 | 1.584 |
| Number of reflections | 10853 | 574 |
| <I/σ(I)> | 10.3 | 1.3 |
| Completeness [%] | 92.9 | 100 |
| Redundancy | 6.5 | 6.7 |
| CC(1/2) | 0.997 | 0.347 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 291.15 | 24.3 mg/ml; 0.1 M MES 6.5; 30 % v/v BCS PEG Smear Low |
