1PW2

APO STRUCTURE OF HUMAN CYCLIN-DEPENDENT KINASE 2

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR571
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-09-01
Detector	MARRESEARCH
Wavelength(s)	1.54
Spacegroup name	P 21 21 21
Unit cell lengths	53.687, 71.799, 72.032
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.930 - 1.950
R-factor	0.213
Rwork	0.213
R-free	0.24900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hcl
RMSD bond length	0.005
RMSD bond angle	22.600 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.000
High resolution limit [Å]	1.950	1.950
Rmerge	0.073	0.235 *
Total number of observations	222716 *
Number of reflections	20576
<I/σ(I)>	16.5
Completeness [%]	97.1 *	98.4 *
Redundancy	10.45

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.8	277	PEG 6000, Na-HEPES, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7-8 (mg/ml)
2	1	reservoir	PEG6000	15 (%)
3	1	reservoir	sodium HEPES	100 (mM)	pH7.8-8.2