5MRB

Crystal structure of human Mps1 (TTK) in complex with Cpd-5

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	70.582, 111.419, 115.025
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	41.390 - 2.200
R-factor	0.1753
Rwork	0.173
R-free	0.21590
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3hmn
RMSD bond length	0.011
RMSD bond angle	1.366
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]	41.390	41.390	2.270
High resolution limit [Å]	2.200	9.070	2.200
Rmerge	0.046	0.021	0.868
Number of reflections	23225
<I/σ(I)>	18.2
Completeness [%]	99.3	95.6	99.8
Redundancy	4.6	4	4.8
CC(1/2)	0.999	0.999	0.702

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.8	291	Protein solution: 200 uM (7.2 mg/mL) Mps1, 250 uM Cpd-5. Reservoir solution: 15.5% (w/v) PEG 350 MME, 10 mM MgCl2, and 100 mM Tris/HCl