3ZS5

Structural basis for kinase selectivity of three clinical p38alpha inhibitors

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2005-09-28
Detector	ADSC QUANTUM 4
Spacegroup name	P 21 21 21
Unit cell lengths	67.492, 70.036, 75.010
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	51.160 - 1.600
R-factor	0.18586
Rwork	0.184
R-free	0.21527
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.011
RMSD bond angle	1.271
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	REFMAC
Refinement software	REFMAC (5.5.0102)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.700	1.690
High resolution limit [Å]	1.600	1.600
Rmerge	0.080	0.880
Number of reflections	44440
<I/σ(I)>	8	2.2
Completeness [%]	93.8	75.3
Redundancy	6.9	5.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5		HANGING DROP, ROOM TEMP, 20 MM HEPES PH7.1, 50 MM NACL, 10 MM DTT, 5% GLYCEROL, 0.1 G/L METHIONINE, 28% PEG 4K,0.1 M MES PH=6.5, 50 MM N-OCTYL-BETAGLUCOSIDE. CRYOPROTECTANT 28% PEG 4K, 0.1M MES PH5.9, 50 MM N-OCTYL-BETAGLUCOSIDE, 20% ETHYLENE GLYCOL.