1PJK

Crystal Structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	283
Detector technology	IMAGE PLATE
Collection date	2002-12-06
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	59.044, 46.502, 64.262
Unit cell angles	90.00, 112.02, 90.00

Refinement procedure

Resolution	17.300 - 2.500
R-factor	0.18792
Rwork	0.180
R-free	0.25700 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	CHAIN A of PDB ENTRY 1JWH
RMSD bond length	0.009
RMSD bond angle	1.120 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	17.300	2.590
High resolution limit [Å]	2.500	2.500
Rmerge	0.118 *	0.602 *
Number of reflections	11207	1136 *
<I/σ(I)>	8.4
Completeness [%]	98.5	99.9
Redundancy	2.3	2.3 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	20 *	PEGmme 5000, ammonium sulfate, MES, adenylyl imidodiphosphate, magnesium chloride, peptide RRRADDSDDDDD, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG5000 MME	30 (%(w/v))
2	1	reservoir	ammonium sulfate	0.2 (M)
3	1	reservoir	MES	0.1 (M)	pH7.5
4	1	drop		2 (mM)
5	1	drop	AMP-PNP	1 (mM)
6	1	drop	peptide	0.62 (mM)