3C8X

Crystal structure of the ligand binding domain of human Ephrin A2 (Epha2) receptor protein kinase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2008-01-11
Detector	RIGAKU RAXIS IV
Spacegroup name	P 31 2 1
Unit cell lengths	92.518, 92.518, 41.291
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	35.000 - 1.950
R-factor	0.16583
Rwork	0.163
R-free	0.22623
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1kgy
RMSD bond length	0.016
RMSD bond angle	1.520
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.000	2.020
High resolution limit [Å]	1.950	1.950
Number of reflections	14975
<I/σ(I)>	15.44	1.8281
Completeness [%]	99.9	98.6
Redundancy	6.8	5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	291.2	AN IN-SITU PROTEOLYSIS STRATEGY WAS USED TO GENERATE HIGH QUALITY CRYSTALS. TRYPSIN WAS ADDED FROM A 1.5 GRAM/L STOCK TO A PROTEIN SAMPLE (AT 6.2 GRAM/L) TO A FINAL TRYPSIN CONC OF 6.2 MICROGRAM/L BEFORE CRYSTAL PLATES WERE SET AT 291.2K. 25% PEG 3350, 0.1 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PH 5.5. PARATONE-N WAS USED AS THE CRYOPROTECTANT, VAPOR DIFFUSION, SITTING DROP