3OBJ

Conformational plasticity of p38 MAP kinase DFG mutants in response to inhibitor binding

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-002+
Temperature [K]	93
Detector technology	IMAGE PLATE
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.54
Spacegroup name	P 21 21 21
Unit cell lengths	68.319, 69.839, 76.088
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.410 - 2.400
R-factor	0.22019
Rwork	0.215
R-free	0.28673
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1zyj
RMSD bond length	0.015
RMSD bond angle	1.780
Data reduction software	d*TREK
Data scaling software	d*TREK
Phasing software	AMoRE
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	33.410	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.092
Number of reflections	25143
<I/σ(I)>	11.2	4.2
Completeness [%]	99.1	96.1
Redundancy	5.19	4.59

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	295	10-15% PEG 4000, 0.1M cacodylic acid, 50 mM n-octyl-beta-D-glucoside, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K