3TCP

Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC569

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	2010-12-10
Detector	MARMOSAIC 300 mm CCD
Spacegroup name	P 1 21 1
Unit cell lengths	51.158, 91.142, 68.356
Unit cell angles	90.00, 100.35, 90.00

Refinement procedure

Resolution	29.020 - 2.690
R-factor	0.228
Rwork	0.225
R-free	0.29800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3brb
RMSD bond length	0.008
RMSD bond angle	1.147
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.5.0110)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.020	2.720
High resolution limit [Å]	2.690	2.690
Rmerge	0.098	0.522
Number of reflections	16603
<I/σ(I)>	14.7	1.5
Completeness [%]	96.3	59.3
Redundancy	3.6	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		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