6GVJ
Human Mps1 kinase domain with ordered activation loop
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 | 2018-04-23 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.966 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 70.825, 102.613, 110.973 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 58.290 - 2.410 |
| R-factor | 0.2028 |
| Rwork | 0.201 |
| R-free | 0.23340 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3hmn |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.018 |
| Data reduction software | xia2 |
| Data scaling software | Aimless (0.6.3) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (refmac_5.8.0222) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 58.290 | 58.290 | 2.470 |
| High resolution limit [Å] | 2.410 | 10.780 | 2.410 |
| Rmerge | 0.086 | 0.039 | 0.524 |
| Rmeas | 0.097 | 0.044 | 0.608 |
| Rpim | 0.045 | 0.020 | 0.301 |
| Total number of observations | 72288 | 916 | 4746 |
| Number of reflections | 15900 | 209 | 1156 |
| <I/σ(I)> | 10.4 | 24.6 | 2.3 |
| Completeness [%] | 99.7 | 98.7 | 99.7 |
| Redundancy | 4.5 | 4.4 | 4.1 |
| CC(1/2) | 0.995 | 0.998 | 0.603 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.2 M Ammonium sulfate 20% (w/v) PEG8000 0.1 M MES-buffer, pH 6.5 |
