3C13

Low 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 X12
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X12
Temperature [K]	100
Detector technology	CCD
Collection date	2007-02-10
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.9537
Spacegroup name	P 1 21 1
Unit cell lengths	58.730, 45.680, 63.240
Unit cell angles	90.00, 111.80, 90.00

Refinement procedure

Resolution	19.700 - 1.950
R-factor	0.1877
Rwork	0.185
R-free	0.23346
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3bqc
RMSD bond length	0.013
RMSD bond angle	1.397
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.700	2.020
High resolution limit [Å]	1.950	1.950
Rmerge	0.112	0.626
Number of reflections	22776
<I/σ(I)>	13.9	2
Completeness [%]	99.9	100
Redundancy	4.5	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.6	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 ammonium acetate, 0.1M sodium citrate, pH 5.6 Crystallization drop: 2 microliters protein/emodin mixture plus 1 microliter reservoir solution, VAPOR DIFFUSION, SITTING DROP, temperature 293K