7B8H

Monoclinic structure of human protein kinase CK2 catalytic subunit in complex with a heparin oligo saccharide

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	2015-07-02
Detector	DECTRIS PILATUS 2M-F
Wavelength(s)	0.8
Spacegroup name	P 1 21 1
Unit cell lengths	58.760, 45.190, 63.460
Unit cell angles	90.00, 111.94, 90.00

Refinement procedure

Resolution	34.788 - 1.340
R-factor	0.1539
Rwork	0.154
R-free	0.16390
Structure solution method	SAD
RMSD bond length	0.011
RMSD bond angle	1.179
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHENIX
Refinement software	PHENIX ((1.13_2998: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	34.790	1.388
High resolution limit [Å]	1.340	1.340
Rmerge	0.039	0.738
Rmeas	0.042	0.799
Rpim	0.016	0.305
Number of reflections	68560	6741
<I/σ(I)>	21.17
Completeness [%]	98.6	97.47
Redundancy	6.8	6.7
CC(1/2)	1.000	0.777

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293.15	1 microliter protein stock solution (8 mg/ml CK2alpha, 2 mM Heparin dodecasaccharide, 285.7 mM NaCl, 15 mM Tris, pH 8.5) was mixed with 2.5 microliter reservoir solution (32 %(w/v) PEG4000, 0.2 M malonate, 0.1 M Tris, pH 7.5). The resulting drop was equilibrated against 800 microliter reservoir solution. After equilibration the crystallization process was initialized by addition of 150 nanoliter micro seeding suspension. CK2alpha/heparin crystals grown in this way were prepared for cryo diffractometry by soaking them into a cryo solution consisting of 32 % (w/v) PEG4000, 0.2 M NaCl, 0.5 mM Heparin dodecasaccharide.