5NAD
TTK kinase domain in complex with BAY 1217389
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 | 70.450, 109.780, 114.330 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 79.190 - 2.800 |
| R-factor | 0.20962 |
| Rwork | 0.206 |
| R-free | 0.28967 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5n7v |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.863 |
| 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] | 79.190 | 2.990 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.093 | 0.936 |
| Rpim | 0.057 | 0.562 |
| Number of reflections | 11158 | 1972 |
| <I/σ(I)> | 7.1 | 1.3 |
| Completeness [%] | 99.4 | 99.1 |
| Redundancy | 4.3 | 4.4 |
| CC(1/2) | 0.991 | 0.611 |
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 |
