6HMQ

STRUCTURE OF PROTEIN KINASE CK2 CATALYTIC SUBUNIT (ISOFORM CK2ALPHA'; CSNK2A2 GENE PRODUCT) IN COMPLEX WITH THE BENZOTRIAZOLE-TYPE INHIBITOR MB002

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID30B
Synchrotron site	ESRF
Beamline	ID30B
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-04-18
Detector	DECTRIS PILATUS3 S 6M
Wavelength(s)	0.8
Spacegroup name	P 1
Unit cell lengths	46.140, 47.220, 50.290
Unit cell angles	113.47, 90.76, 90.27

Refinement procedure

Resolution	46.133 - 0.970
R-factor	0.1203
Rwork	0.120
R-free	0.13170
Structure solution method	AB INITIO PHASING
RMSD bond length	0.011
RMSD bond angle	1.116
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	Arcimboldo
Refinement software	PHENIX ((1.14_3260: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	43.113	1.005
High resolution limit [Å]	0.970	0.970
Rmerge	0.045	1.504
Rmeas	0.048	1.631
Rpim	0.018	0.625
Number of reflections	213727	20760
<I/σ(I)>	20.27	1.16
Completeness [%]	89.6	78.71
Redundancy	6.9	6.7
CC(1/2)	0.999	0.526

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293.15	180 MICROLITERs ENZYME STOCK SOLUTION (6 MG/ML IN 500 MM NACL, 25 MM TRIS/HCL, PH 8.5) WERE MIXED and Incubated WITH 20 MIKROLITERS of a STOCK SOLUTION of the inhibitor 4B0 (10 MM 4B0 IN DMSO). 20 MICROLITERS OF resulting solution WERE MIXED WITH 10 MICROLITERS OF RESERVOIR SOLUTION (900 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 on the plate. THE DROPLETS WERE EQUILIBRATED AT 293.15 K using the sitting drop variant of the VAPOR DIFFUSION method.