3G51

Structural diversity of the active conformation of the N-terminal kinase domain of p90 ribosomal S6 kinase 2

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	100
Detector technology	CCD
Collection date	2008-03-07
Detector	ADSC QUANTUM 315
Wavelength(s)	0.979
Spacegroup name	P 21 21 21
Unit cell lengths	51.167, 51.381, 140.873
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	36.300 - 1.800
R-factor	0.216
Rwork	0.204
R-free	0.24800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1vzo
RMSD bond length	0.003
RMSD bond angle	0.600
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHENIX
Refinement software	PHENIX

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	36.000	1.860
High resolution limit [Å]	1.800	1.800
Rmerge	0.091
Number of reflections	35092
Completeness [%]	99.4	94.8
Redundancy	6.2	5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	The diluted protein at different concentrations (2.5 mg/ml 10 mg/ml) was mixed at a 2:1 ratio with precipitant solution (6%-10% PEG 3350, 0.2 M proline, 0.1 M Hepes pH 7.5). , VAPOR DIFFUSION, SITTING DROP, temperature 293K