9QUI
Ni(II)-bound de novo protein scaffold TFD-EH
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X13 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-10-29 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9763 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 76.740, 76.740, 71.210 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 2.100 |
| R-factor | 0.18679 |
| Rwork | 0.185 |
| R-free | 0.22291 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 1.200 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.200 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.042 | 0.640 |
| Number of reflections | 13957 | 1826 |
| <I/σ(I)> | 19.4 | 2.3 |
| Completeness [%] | 96.1 | 98.7 |
| Redundancy | 5.2 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 0.05 M Imidazole, 12% PEG 6000 |
