4RIY

Crystal structure of an EGFR/HER3 kinase domain heterodimer containing the cancer-associated HER3-E909G mutation

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.3.1
Synchrotron site	ALS
Beamline	8.3.1
Temperature [K]	100
Detector technology	CCD
Collection date	2014-07-27
Detector	ADSC QUANTUM 315r
Wavelength(s)	1.115867
Spacegroup name	P 1 21 1
Unit cell lengths	65.334, 155.140, 87.297
Unit cell angles	90.00, 110.93, 90.00

Refinement procedure

Resolution	56.200 - 2.981
R-factor	0.2212
Rwork	0.216
R-free	0.26700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2GS6 AND 3KEX
RMSD bond length	0.005
RMSD bond angle	1.093
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine: 1.9_1692))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	60.000	3.210
High resolution limit [Å]	2.981	3.000
Rmerge	0.176	0.573
Number of reflections	32340
<I/σ(I)>	6.5	2.7
Completeness [%]	99.5	99.9
Redundancy	3.8	3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	10 mg/mL protein, 0.1M HEPES pH 7.5, 15% PEG-5000 MME, 5mM magnesium chloride, 0.5M ammonium acetate, 2mM AMP-PNP, 1mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K