1URZ

Low pH induced, membrane fusion conformation of the envelope protein of tick-borne encephalitis virus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X06SA
Synchrotron site	SLS
Beamline	X06SA
Temperature [K]	100
Detector technology	CCD
Collection date	2003-06-15
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	121.500, 142.900, 173.600
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.000 - 2.700
R-factor	0.207
Rwork	0.207
R-free	0.24200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1svb
RMSD bond length	0.007
RMSD bond angle	25.900 *
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.800
High resolution limit [Å]	2.700	2.700
Rmerge	0.111	0.455
Total number of observations	306381 *
Number of reflections	80896
<I/σ(I)>	5.4	2
Completeness [%]	96.9	83.9
Redundancy	3.8	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.5		Stiasny, K., (2004) J. Virol., 78, 3178. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	2-5 (mg/ml)
2	1	reservoir	sodium acetate	0.1 (M)	pH4.5
3	1	reservoir	PEG2000	20-30 (%)