5K0X

Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC2541

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)	1.0000
Spacegroup name	P 1 21 1
Unit cell lengths	51.671, 91.599, 69.769
Unit cell angles	90.00, 102.37, 90.00

Refinement procedure

Resolution	27.864 - 2.231
R-factor	0.189
Rwork	0.185
R-free	0.23900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3brb
RMSD bond length	0.014
RMSD bond angle	1.296
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	PHENIX (1.10.1_2155)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.270
High resolution limit [Å]	2.230	2.230
Rmerge	0.076	0.661
Number of reflections	30743
<I/σ(I)>	8.8	2
Completeness [%]	99.9	99
Redundancy	4.2	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	286	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).