9HYK
Crystal structure of Trypanosoma brucei trypanothione reductase (TbTR) bound to PROTAC-1
This is a non-PDB format compatible entry.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 11.2C |
| Synchrotron site | ELETTRA |
| Beamline | 11.2C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-03-31 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 101.700, 63.820, 169.910 |
| Unit cell angles | 90.00, 98.10, 90.00 |
Refinement procedure
| Resolution | 168.220 - 2.090 |
| R-factor | 0.19979 |
| Rwork | 0.197 |
| R-free | 0.24314 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.515 |
| Data reduction software | autoPROC |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 168.220 | 2.230 |
| High resolution limit [Å] | 2.090 | 2.090 |
| Number of reflections | 124478 | 39544 |
| <I/σ(I)> | 9.4 | |
| Completeness [%] | 100.0 | |
| Redundancy | 5.3 | |
| CC(1/2) | 0.997 | 0.977 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 13-15% PEG3350, 22-24% MPD, 40 mM imidazole pH 8.0, 50 mM NaBr |
