5N9S
TTK kinase domain in complex with BAY 1161909
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-01-27 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.966 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 71.580, 112.180, 113.850 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 60.340 - 2.300 |
| R-factor | 0.19362 |
| Rwork | 0.191 |
| R-free | 0.24485 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5n7v |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.796 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 60.600 | 2.390 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.077 | 0.575 |
| Rpim | 0.037 | 0.251 |
| Number of reflections | 20720 | 2300 |
| <I/σ(I)> | 11.2 | 2.7 |
| Completeness [%] | 99.9 | 99.6 |
| Redundancy | 5.8 | 5.9 |
| CC(1/2) | 0.997 | 0.917 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.3 | 293 | 32 - 37% PEG400 (Acros, Geel, Belgium), 0.1 M Na/K phosphate pH 6.3 and 250 mM NaCl.pH 6.3 |
