3BQC

High pH-value crystal structure of emodin in complex with the catalytic subunit of protein kinase CK2

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2007-02-10
Detector	MAR scanner 345 mm plate
Spacegroup name	P 1 21 1
Unit cell lengths	58.870, 45.740, 63.500
Unit cell angles	90.00, 111.78, 90.00

Refinement procedure

Resolution	34.260 - 1.500
R-factor	0.13324
Rwork	0.130
R-free	0.19734
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1pjk
RMSD bond length	0.012
RMSD bond angle	1.390
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	34.300	1.550
High resolution limit [Å]	1.500	1.500
Rmerge	0.036	0.607
Number of reflections	50159
<I/σ(I)>	35.3	1.9
Completeness [%]	99.1	98.8
Redundancy	3.7	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	Protein stock solution: 10mg/ml protein in 500mM NaCl, 25mM Tris/HCl, pH 8.5 Emodin stock solution: 10mM in water Protein/emodin mixture: equal volumes of protein and emodin stock solutions were mixed and equillibrated for 30 min prior to crystallization Reservoir: 30% PEG4000, 0.2M lithium sulfate, 0.1M Tris/HCl, pH 8.5 Crystallization drop: 2 mikroliters protein/emodin mixture plus 1 mikroliter reservoir solution, VAPOR DIFFUSION, SITTING DROP, temperature 293K