31HP
Crystal structure of tau tubulin kinase 2 (TTBK2) 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 I04 |
| Synchrotron site | Diamond |
| Beamline | I04 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-11-19 |
| Detector | DECTRIS EIGER2 X 16M |
| Wavelength(s) | 0.97628 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 38.989, 70.387, 55.136 |
| Unit cell angles | 90.00, 100.46, 90.00 |
Refinement procedure
| Resolution | 42.950 - 1.500 |
| R-factor | 0.149993543044 |
| Rwork | 0.148 |
| R-free | 0.18696 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.755 |
| 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] | 42.950 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.047 | 0.577 |
| Number of reflections | 46597 | 2288 |
| <I/σ(I)> | 17.5 | 2.7 |
| Completeness [%] | 99.4 | 99.9 |
| Redundancy | 6.9 | 7 |
| CC(1/2) | 1.000 | 0.896 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | Protein concentration: 5.75 mg/ml Crystallization buffer: 25% PEG 3350, 0.2 M ammonium acetate, 0.1 M HEPES pH 7.5. |
