7UY3

Crystal structure of human Fgr tyrosine kinase in complex with TL02-59

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	PIXEL
Collection date	2018-03-29
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.9757
Spacegroup name	P 65 2 2
Unit cell lengths	151.285, 151.285, 130.518
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	46.233 - 2.990
R-factor	0.2074
Rwork	0.203
R-free	0.24730
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2src
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.14_3260)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	46.233	46.233	3.070
High resolution limit [Å]	2.990	13.370	2.990
Rmerge	0.125	0.079	0.804
Rmeas	0.131	0.084	0.840
Number of reflections	33705	250	1311
<I/σ(I)>	11.89	21.97	2.07
Completeness [%]	99.9	95.8	99.8
Redundancy	10.954	8.804	11.23
CC(1/2)	0.997	0.996	0.909

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.5	277	For co-crystallization with TL02-59, Fgr (3.2 mg/mL in 20 mM Tris-HCl, pH 8.3, 100 mM NaCl, and 2 mM TCEP) was mixed with 10 mM TL02-59 (in 100% DMSO) to a final concentration of 120 microM (0.6% DMSO final) and incubated for thirty minutes at 298 K. Diffraction quality crystals were grown by sitting- and hanging-drop vapor diffusion at 277 K by mixing Fgr/TL02-59 in a 1:1 ratio with the mother liquor (0.1 M HEPES, pH 7.5, 0.8 M sodium phosphate, 0.8 M potassium phosphate and 1% 1,2-butanediol)