4AN9

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 BL9-1
Synchrotron site	SSRL
Beamline	BL9-1
Temperature [K]	100
Detector technology	CCD
Collection date	2005-05-10
Detector	ADSC QUANTUM 315r
Spacegroup name	P 61
Unit cell lengths	108.653, 108.653, 49.394
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	49.400 - 2.800
R-factor	0.20522
Rwork	0.200
R-free	0.31259
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	UNPUBLISHED MEK1-ATP COMPLEX
RMSD bond length	0.020
RMSD bond angle	2.260
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.390	2.950
High resolution limit [Å]	2.800	2.800
Rmerge	0.120	0.820
Number of reflections	8366
<I/σ(I)>	11.3	2.3
Completeness [%]	99.8	100
Redundancy	5.4	5.5

Crystallization Conditions

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