9HK5

Structure of a mutant of human protein kinase CK2alpha' that equals its isoenzyme CK2alpha in affinity to the regulatory subunit CK2beta

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	2024-11-28
Detector	DECTRIS EIGER2 X 9M
Wavelength(s)	0.873128
Spacegroup name	P 1
Unit cell lengths	46.788, 47.804, 50.579
Unit cell angles	111.76, 90.22, 91.55

Refinement procedure

Resolution	46.970 - 1.491
R-factor	0.1748
Rwork	0.174
R-free	0.20380
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	0.793
Data reduction software	autoPROC
Data scaling software	autoPROC
Phasing software	PHASER
Refinement software	PHENIX (1.21_5207)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.971	1.672
High resolution limit [Å]	1.491	1.491
Rmerge	0.104	0.775
Rmeas	0.129	0.944
Rpim	0.076	0.533
Number of reflections	44234	2189
<I/σ(I)>	7.7	1.6
Completeness [%]	88.3	11.4
Redundancy	2.8	3
CC(1/2)	0.992	0.447

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	protein stock solution: 5 mg/ml protein, 500 mM NaCl, 25 mM Tris/HCl, pH 8.5; protein/inhibitor mixture: 19 mikroliter protein stock solution plus 1 mikroliter 20 mM CX-4945 in DMSO; reservoir: 900 mM LiCL, 28 % (w/v) PEG 6000, 250 mM Tris/HCl, pH 8.5; crystallization drop: 2 mikroliter reservoir + 4 mikroliter protein/inhibitor mixture; initial crystals were optimized by micro seeding