4MHA

Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC1817

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-B
Synchrotron site	APS
Beamline	23-ID-B
Temperature [K]	100
Detector technology	CCD
Collection date	2012-04-08
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.03320
Spacegroup name	P 1 21 1
Unit cell lengths	51.142, 91.460, 69.932
Unit cell angles	90.00, 100.23, 90.00

Refinement procedure

Resolution	40.066 - 2.590
R-factor	0.2465
Rwork	0.241
R-free	0.29390
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3tcp
RMSD bond length	0.002
RMSD bond angle	0.477
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]	40.070	2.610
High resolution limit [Å]	2.590	2.590
Rmerge	0.117	0.711
Number of reflections	19608
<I/σ(I)>	11.8	2
Completeness [%]	99.7	97.4
Redundancy	4.2	4

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