4AN3

Crystal structures of human MEK1 with carboxamide-based allosteric inhibitor XL518 (GDC-0973), or related analogs.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL11-1
Synchrotron site	SSRL
Beamline	BL11-1
Temperature [K]	100
Detector technology	CCD
Collection date	2005-03-31
Detector	MARMOSAIC 325 mm CCD
Spacegroup name	P 61
Unit cell lengths	108.659, 108.659, 50.113
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	44.220 - 2.100
R-factor	0.22865
Rwork	0.226
R-free	0.28311
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	UNPUBLISHED MEK1-ATP STRUCTURE
RMSD bond length	0.020
RMSD bond angle	2.100
Data reduction software	d*TREK
Data scaling software	d*TREK
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	44.230	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.070	0.460
Number of reflections	19901
<I/σ(I)>	8.1	2.2
Completeness [%]	99.5	100
Redundancy	3.2	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.9		SITTING DROP VAPOR DIFFUSION VS. 26.5 % PEG-2000 MME, 0.1 M TRIMETHYLAMINE N-OXIDE, 0.1 M TRIS (PH 8.9)