1B4F

OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	100
Collection date	1998-08
Wavelength(s)	0.96859, 0.97966, 0.97982, 1.0000
Spacegroup name	P 41
Unit cell lengths	73.897, 73.897, 104.547
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	26.000 - 1.950
R-factor	0.228
Rwork	0.228
R-free	0.27300
Structure solution method	MAD
RMSD bond length	0.028
RMSD bond angle	22.100 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS (0.4)
Refinement software	CNS (0.4)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	26.000	2.020
High resolution limit [Å]	1.950	1.950
Rmerge	0.047 *	0.163 *
Total number of observations	223269 *
Number of reflections	39547
<I/σ(I)>	17.6	6.84
Completeness [%]	96.5	98.7
Redundancy	5.6	5.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7	4 *	pH 7.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	reservoir	HEPES	100 (mM)
3	1	reservoir	Tris	10 (mM)
4	1	reservoir	dithiothreitol	20 (mM)
5	1	reservoir		30 (mM)
6	1	reservoir	PEG1000	26-30 (%)