4MH7

Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC1896

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2012-06-13
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97921
Spacegroup name	P 1 21 1
Unit cell lengths	50.874, 90.864, 69.587
Unit cell angles	90.00, 99.98, 90.00

Refinement procedure

Resolution	32.060 - 2.510
R-factor	0.2283
Rwork	0.223
R-free	0.27930
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3brb
RMSD bond length	0.003
RMSD bond angle	0.659
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine: dev_1468))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	32.060	2.530
High resolution limit [Å]	2.510	2.510
Rmerge	0.125	0.564
Number of reflections	20799
<I/σ(I)>	10.7	2.2
Completeness [%]	97.7	81.1
Redundancy	4.1	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	288	Protein: 32.5 mg/mL in 20 mM Tris pH 8.0, 500mM sodium chloride, 2mM beta-mercaptoethanol, incubated with inhibitor (2.5 mM final concentration) overnight, mixed 1:1 with crystallization solution (27-33% (v/v) Peg400, 200 mM magnesium chloride, 100 mM Tris pH 8.5), VAPOR DIFFUSION, SITTING DROP, temperature 288K