8G4K
Complex of TbRII mini protein binder bound to the TbRII ECD
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-02-03 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 47.983, 57.175, 78.798 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.280 - 1.240 |
| Rwork | 0.181 |
| R-free | 0.19580 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1m9z |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 78.800 | 1.270 |
| High resolution limit [Å] | 1.240 | 1.240 |
| Rmerge | 0.052 | 0.898 |
| Rmeas | 0.055 | |
| Rpim | 0.018 | 0.662 |
| Number of reflections | 61539 | 2727 |
| <I/σ(I)> | 18.9 | 0.6 |
| Completeness [%] | 95.7 | 53.4 |
| Redundancy | 8.9 | 2.3 |
| CC(1/2) | 1.000 | 0.425 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 300 | 20% PEG5000 MME, 0.2-0.4 M ammonium sulfate, 0.1 M Tris, pH 7.4, 16-32% glycerol |
