3MPA

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Temperature [K]	93
Detector technology	CCD
Detector	ADSC QUANTUM 4
Wavelength(s)	0.98
Spacegroup name	P 21 21 21
Unit cell lengths	65.471, 74.144, 77.184
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.340 - 2.100
R-factor	0.23502
Rwork	0.230
R-free	0.28933
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1zyj
RMSD bond length	0.013
RMSD bond angle	1.467
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.042	0.266
Number of reflections	22530
<I/σ(I)>	31	2.9
Completeness [%]	95.0	79.6
Redundancy		2.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	295	10-20% PEG 4000, 0.1 M cacodylic acid, 50 mM n-octyl-beta-D-glucoside, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K