5K0K

Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC2434

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-BM
Synchrotron site	APS
Beamline	22-BM
Temperature [K]	100
Detector technology	CCD
Collection date	2012-12-12
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.9792
Spacegroup name	P 1 21 1
Unit cell lengths	51.072, 91.315, 69.203
Unit cell angles	90.00, 100.42, 90.00

Refinement procedure

Resolution	34.547 - 2.545
R-factor	0.2035
Rwork	0.198
R-free	0.25430
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3brb
RMSD bond length	0.004
RMSD bond angle	0.720
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	PHENIX (dev_1261)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	34.550	2.570
High resolution limit [Å]	2.545	2.545
Rmerge	0.086	0.686
Number of reflections	20516
<I/σ(I)>	7.9	1.9
Completeness [%]	99.8	96
Redundancy	4.2	3.8

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).