6MEP

Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC3437

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	2013-10-19
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.0743
Spacegroup name	P 1 21 1
Unit cell lengths	51.366, 92.048, 69.690
Unit cell angles	90.00, 101.67, 90.00

Refinement procedure

Resolution	37.069 - 2.893
R-factor	0.2099
Rwork	0.205
R-free	0.26820
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.002
RMSD bond angle	0.643
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	PHENIX (1.10.1_2155)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.920
High resolution limit [Å]	2.893	2.893
Rmerge	0.142	0.771
Number of reflections	14260	337
<I/σ(I)>	5.7
Completeness [%]	99.9	98.5
Redundancy	4.2	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	285.2	Protein at 32.5 mg/mL (in 20 mM Tris pH 8.0, 500 mM NaCl, 2mM BME) was incubated overnight with inhibitor at 2.5 mM final concentration, and then was mixed 1:1 with crystallization solution (27-33% (v/v) Peg 400, 200 mM MgCl2, 100 mM Tris pH 8.5).