5N9L

Crystal structure of human Protein kinase CK2 catalytic subunit in complex with the ATP-competitive dibenzofuran inhibitor TF (4b)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X06DA
Synchrotron site	SLS
Beamline	X06DA
Temperature [K]	100
Detector technology	PIXEL
Collection date	2012-10-12
Detector	DECTRIS PILATUS 2M
Wavelength(s)	0.99987
Spacegroup name	P 1 21 1
Unit cell lengths	57.437, 45.706, 63.187
Unit cell angles	90.00, 110.94, 90.00

Refinement procedure

Resolution	36.135 - 1.790
R-factor	0.1653
Rwork	0.164
R-free	0.19920
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2pvr
RMSD bond length	0.003
RMSD bond angle	0.664
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.11.1_2575: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	36.140	1.830
High resolution limit [Å]	1.790	1.790
Rmerge	0.056	0.545
Number of reflections	27738	1127
<I/σ(I)>	11.3	1.5
Completeness [%]	95.1	65.9
Redundancy	3.5	2.9
CC(1/2)	0.998	0.760

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.6	293	Prior to the crystallization TF was solubilized in 100 % DMSO in a concentration of 10 mM. TF was mixed with human CK2alpha (construct 1-335; 8-10 mg/ml in 500 mM sodium chloride, 25 mM Tris/HCl pH 8.5) in a ratio of 1:5. After a short time of incubation this mixture was mixed with reservoir solution [32 % (w/v) PEG4000, 0.2 M ammonium acetate, 0.1 M citrate pH 5.6] in a ratio of 5:2. 3.5 microliter of the resulting mixture was then equilibrated against the reservoir solution. The crystal growth was induced by seeding with 150 nanoliter seed suspension after an equilibration time of two days.