1I9W

CRYSTAL STRUCTURE OF THE FUSION GLYCOPROTEIN E1 FROM SEMLIKI FOREST VIRUS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-3
Synchrotron site	ESRF
Beamline	ID14-3
Temperature [K]	100
Detector technology	CCD
Collection date	1998-01-22
Detector	MARRESEARCH
Wavelength(s)	0.945
Spacegroup name	P 64 2 2
Unit cell lengths	79.460, 79.460, 334.760
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	15.000 - 3.000
R-factor	0.275 *
Rwork	0.275
R-free	0.33700 *
Structure solution method	MIR
Data reduction software	DENZO
Data scaling software	CCP4 ((SCALA))
Phasing software	MLPHARE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000
High resolution limit [Å]	3.000	3.000
Rmerge	0.082	0.252
Number of reflections	11519
<I/σ(I)>	7.5	3
Completeness [%]	86.5
Redundancy	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Batch method *	8	294	Wengler, G., (1999) Virology, 257, 472. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	20 (mg/ml)
2	1	1	PEG8000	1-5 (%(w/v))
3	1	2	pure paraffin oil