7ATV

Structure of protein kinase ck2 catalytic subunit (csnk2a2 gene product) in complex with the bivalent inhibitor KN2

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	BESSY BEAMLINE 14.2
Synchrotron site	BESSY
Beamline	14.2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2019-06-16
Detector	DECTRIS PILATUS3 S 2M
Wavelength(s)	0.91840
Spacegroup name	P 1
Unit cell lengths	46.783, 47.560, 50.998
Unit cell angles	66.80, 88.96, 88.75

Refinement procedure

Resolution	33.280 - 0.980
R-factor	0.127
Rwork	0.127
R-free	0.14110
Structure solution method	AB INITIO PHASING
RMSD bond length	0.012
RMSD bond angle	1.171
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.18.2_3874)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	33.281	1.020
High resolution limit [Å]	0.964	0.964
Rmerge	0.051	0.907
Rmeas	0.059	1.057
Rpim	0.030	0.540
Number of reflections	190713	9537
<I/σ(I)>	12.4	1.3
Completeness [%]	78.3	25.4
Redundancy	3.7	3.7
CC(1/2)	0.999	0.514

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	Reservoir composition: 28 % (w/v) PEG6000, 0.9 M LiCl, 0.1 M, Tris/HCl, pH 8.5; drop composition prior to equilibration: 0.01 ml reservoir solution + 0.02 ml CK2alpha' (mutant Cys336Ser) /inhibitor MB002 mixture (0.180 ml 6 mg/ml CK2alpha'Cys336Ser, 0.5 M NaCl, 25 mM Tris/HCl, pH 8.5, mixed and pre-equilibrated with 0.02 ml 10 mM MB002 in dimethyl sulfoxide); the initial inhibitor MB002 was replaced by the bivalent inhibitor KN2 by extensive crystal soaking.