5NA0
TTK kinase domain in complex with a PEG-linked pyrimido-indolizine
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 | 2016-03-24 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.966 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 71.100, 113.280, 115.810 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 60.590 - 2.900 |
| R-factor | 0.21319 |
| Rwork | 0.207 |
| R-free | 0.27092 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5n7v |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.861 |
| 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] | 80.980 | 3.080 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.116 | 1.085 |
| Rpim | 0.066 | 0.642 |
| Number of reflections | 10632 | 1662 |
| <I/σ(I)> | 7.7 | 1.2 |
| Completeness [%] | 99.5 | 98.5 |
| Redundancy | 4.4 | 4.3 |
| CC(1/2) | 0.997 | 0.647 |
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 |
