1MQB

Crystal Structure of Ephrin A2 (ephA2) Receptor Protein Kinase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.3
Synchrotron site	ALS
Beamline	5.0.3
Temperature [K]	100
Detector technology	CCD
Collection date	2001-12-12
Detector	ADSC QUANTUM 4
Wavelength(s)	1.0
Spacegroup name	P 32 2 1
Unit cell lengths	72.127, 72.127, 241.623
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	63.000 * - 2.300
R-factor	0.23619
Rwork	0.236
R-free	0.28900 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1jpa
RMSD bond length	0.021 *
RMSD bond angle	2.110 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC (5.1.19)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	63.000 *	2.360
High resolution limit [Å]	2.300	2.300
Rmerge	0.057	0.485
Number of reflections	35483
<I/σ(I)>	11.5	2
Completeness [%]	95.0 *	78 *
Redundancy	4.1	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.6 *	4 *	Ethylene Glycol, PEG 10K, HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10.7 (mg/ml)
2	1	drop	Tris-HCl	50 (mM)	pH7.6
3	1	drop		250 (mM)
4	1	drop	EDTA	1 (mM)
5	1	drop	dithiothreitol	1 (mM)
6	1	reservoir	HEPES	0.1 (M)	pH7.5
7	1	reservoir	PEG10000	10 (%)
8	1	reservoir	ethylene glycol	8 (%)