31HO
Crystal structure of tau tubulin kinase 1 (TTBK1) in complex with compound 62
This is a non-PDB format compatible entry.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2025-01-20 |
| Detector | DECTRIS EIGER2 XE 16M |
| Wavelength(s) | 0.97628 |
| Spacegroup name | I 1 2 1 |
| Unit cell lengths | 49.756, 38.830, 162.875 |
| Unit cell angles | 90.00, 93.94, 90.00 |
Refinement procedure
| Resolution | 48.400 - 2.700 |
| R-factor | 0.254544126157 |
| Rwork | 0.252 |
| R-free | 0.30648 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.102 |
| Data reduction software | autoPROC |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 81.240 | 2.830 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.186 | 1.604 |
| Rmeas | 0.201 | 1.726 |
| Rpim | 0.075 | 0.633 |
| Number of reflections | 8765 | 1158 |
| <I/σ(I)> | 6.5 | 1.5 |
| Completeness [%] | 99.6 | 100 |
| Redundancy | 7 | 7.3 |
| CC(1/2) | 0.994 | 0.793 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | Protein concentration: 8.4 mg/ml Crystallization buffer: 20% PEG 3350, 0.2 M sodium acetate, 0.1 M Tris pH 8.0 |
