5LJJ
Crystal structure of human Mps1 (TTK) in complex with Reversine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-3 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-3 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-04-16 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.96771 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 70.852, 109.570, 113.209 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.010 - 3.000 |
| R-factor | 0.2281 |
| Rwork | 0.224 |
| R-free | 0.26780 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3hmn |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.071 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.25) |
| Phasing software | PHASER (2.6.1) |
| Refinement software | REFMAC (refmac_5.8.0155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 41.010 | 41.010 | 3.180 |
| High resolution limit [Å] | 3.000 | 9.000 | 3.000 |
| Rmerge | 0.102 | 0.025 | 0.932 |
| Rmeas | 0.115 | 0.029 | 1.065 |
| Rpim | 0.051 | 0.013 | 0.499 |
| Total number of observations | 40889 | 1583 | 5782 |
| Number of reflections | 9005 | ||
| <I/σ(I)> | 10.5 | 42.2 | 1.3 |
| Completeness [%] | 99.0 | 96.6 | 98.1 |
| Redundancy | 4.5 | 4.3 | 4 |
| CC(1/2) | 0.998 | 0.999 | 0.785 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | Protein sollution: 200 uM (7.2 mg/mL) mps1, 250 uM reversine. Reservoir solution: 7.6% (w/v) PEG 350 MME, 0.5 mM MgCl2, and 100 mM Tris/HCl |
