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 |