5N9K

Crystal structure of human Protein kinase CK2 catalytic subunit in complex with the ATP-competitive, tight-binding dibenzofuran inhibitor TF107 (5)

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	57.876, 45.670, 63.753
Unit cell angles	90.00, 111.14, 90.00

Refinement procedure

Resolution	36.220 - 1.643
R-factor	0.1648
Rwork	0.164
R-free	0.18430
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2pvr
RMSD bond length	0.004
RMSD bond angle	0.680
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]	45.670	1.670
High resolution limit [Å]	1.640	1.640
Rmerge	0.036	0.645
Number of reflections	37660	1606
<I/σ(I)>	17	1.6
Completeness [%]	99.0	87
Redundancy	3.3	2.8
CC(1/2)		0.716

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.6	293	Prior to the crystallization the inhibitor was solubilized in 100 % DMSO in a concentration of 10 mM. Then, this inhibitor stock solution was mixed in a Ratio of 1:10 with human CK2alpha (construct 1-335; solved with a Protein concentration of 8-10 mg/ml in 500 mM sodium chloride, 25 mM Tris/HCl pH 8.5). After a short time of incubation this mixture were mixed with reservoir solution [32 % (w/v) PEG4000, 0.2 M ammonium acetate, 0.1 M citrate pH 5.6] in a ratio of 2.5:1. 3.5 microliter of this final 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.