9QUP
Tb(III)-bound de novo protein scaffold TFD-EE MPNN
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 | 2023-11-24 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.976 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 42.980, 66.440, 94.370 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.950 |
| R-factor | 0.1974 |
| Rwork | 0.196 |
| R-free | 0.22585 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| 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 | 2.050 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.059 | 0.837 |
| Number of reflections | 20002 | 2681 |
| <I/σ(I)> | 16.3 | 2.5 |
| Completeness [%] | 98.2 | 96.1 |
| Redundancy | 5.4 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 0.1 M TRIS-HCL, 0.2 M NaCl, 25% PEG 3350 |
