2I2O

Crystal Structure of an eIF4G-like Protein from Danio rerio

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	CCD
Collection date	2006-08-04
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97925
Spacegroup name	C 1 2 1
Unit cell lengths	317.796, 40.948, 40.917
Unit cell angles	90.00, 90.26, 90.00

Refinement procedure

Resolution	40.612 - 1.920
R-factor	0.192
Rwork	0.190
R-free	0.23500
Structure solution method	SAD
RMSD bond length	0.015
RMSD bond angle	1.357
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	40.612	40.610	1.990
High resolution limit [Å]	1.920	4.140	1.920
Rmerge	0.074	0.054	0.245
Number of reflections	39789
<I/σ(I)>	13.377		5.769
Completeness [%]	97.5	100	95.5
Redundancy	6.4	7.1	5.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	PROTEIN SOLUTION (10 MG/ML PROTEIN, 0.050 M SODIUM CHLORIDE, 0.003 M SODIUM AZIDE, 0.0003 M TCEP, 0.005 M BisTris PH 7.0) MIXED IN A 1:1 RATIO WITH THE WELL SOLUTION (7% PEG 4K, 0.40 M sodium chloride, 0.1 M MES/Acetate pH 5.5) CRYOPROTECTED WITH 10% PEG 4K, 0.1 M MES/Acetate pH 5.5, 25% Ethylene glycol, vapor diffusion, hanging drop, temperature 293K