6HMD

STRUCTURE OF PROTEIN KINASE CK2 CATALYTIC SUBUNIT (ISOFORM CK2ALPHA'; CSNK2A2 gene product) IN COMPLEX WITH THE INDENOINDOLE-TYPE INHIBITOR AR18

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Collection date	2017-11-23
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.920042
Spacegroup name	P 1
Unit cell lengths	44.890, 45.820, 48.520
Unit cell angles	113.02, 89.21, 91.18

Refinement procedure

Resolution	22.327 - 1.000
R-factor	0.1496
Rwork	0.149
R-free	0.17180
Structure solution method	AB INITIO PHASING
RMSD bond length	0.022
RMSD bond angle	1.317
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	Arcimboldo
Refinement software	PHENIX ((1.13_2998: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	44.880	1.036
High resolution limit [Å]	1.000	1.000
Rmerge	0.047	1.028
Rmeas	0.055	1.189
Rpim	0.028	0.597
Number of reflections	177359	17032
<I/σ(I)>	15.67	1.36
Completeness [%]	92.2	88.55
Redundancy	3.9	4
CC(1/2)	0.999	0.557

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293.15	180 MICROLITER ENZYME STOCK SOLUTION (6 MG/ML IN 500 MM NACL, 25 MM TRIS/HCL, PH 8.5) WAS MIXED and incubated WITH 20 MIKROLITER of a STOCK SOLUTION of the inhibitor 4B0 (10 MM 4B0 IN DMSO). 20 MICROLITERS OF the resulting solution WAS MIXED WITH 10 MICROLITERS OF RESERVOIR SOLUTION (700 MM LICL, 28 % (W/V) PEG 6000, 100 MM TRIS/HCL, PH 8.5) IN EACH WELL OF A CRYSTALLIZATION PLATE. A SINGLE MACROSEED, grown UNDER THE SAME CONDITIONS, WAS ADDED TO EACH DROPLET of the plate. THE DROPLETS WERE EQUILIBRATED AT 293.15 K using the sitting drop variant of the VAPOR DIFFUSION method. This procedure generated large single crystals of a CK2alpha'/4B0 complex. Afterwards, the inhibitor 4B0 was exchanged against AR18 by an extensive soaking procedure of several steps.