9QUL
Zn(II)-bound de novo protein scaffold TFD-EH T87E
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 | 76.240, 76.240, 70.250 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 1.900 |
| R-factor | 0.18333 |
| Rwork | 0.181 |
| R-free | 0.21925 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 1.144 |
| 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 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.058 | 0.665 |
| Number of reflections | 18249 | 2630 |
| <I/σ(I)> | 9.3 | 2 |
| Completeness [%] | 96.0 | 98.2 |
| Redundancy | 2.9 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 0.05 Imidazole, 16% PEG 6000 |
