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 |