3MH2

Mutagenesis of p38 MAP kinase establishes key roles of Phe169 in function and structural dynamics and reveals a novel DFG-out state

Replaces:  2PTO

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
Collection date	2004-08-16
Detector	ADSC QUANTUM 4
Wavelength(s)	0.98
Spacegroup name	P 21 21 21
Unit cell lengths	66.180, 73.970, 76.800
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	25.070 - 2.300
R-factor	0.24694
Rwork	0.241
R-free	0.31844
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1zyj
RMSD bond length	0.015
RMSD bond angle	1.575
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.480
High resolution limit [Å]	2.300	2.300
Rmerge	0.061	0.314
Number of reflections	16649
<I/σ(I)>	9.9	2.5
Completeness [%]	96.5	98.3
Redundancy	3.2	3.2

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