4M3Q

Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC1917

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	50.924, 91.120, 69.699
Unit cell angles	90.00, 99.81, 90.00

Refinement procedure

Resolution	34.740 - 2.718
R-factor	0.2483
Rwork	0.243
R-free	0.29580
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	3tcp
RMSD bond length	0.003
RMSD bond angle	0.653
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHENIX
Refinement software	PHENIX ((phenix.refine: dev_1439))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	34.740	2.730
High resolution limit [Å]	2.710	2.710
Rmerge	0.110	0.570
Number of reflections	16507
<I/σ(I)>	11.6	2.3
Completeness [%]	97.5	100
Redundancy	4.1	4.2

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, 500 mM sodium chloride, 2 mM 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, VAPOR DIFFUSION, SITTING DROP