1IHM

CRYSTAL STRUCTURE ANALYSIS OF NORWALK VIRUS CAPSID

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F1
Synchrotron site	CHESS
Beamline	F1
Temperature [K]	300
Detector technology	IMAGE PLATE
Collection date	1997-10-01
Detector	FUJI
Wavelength(s)	0.9080
Spacegroup name	P 42 21 2
Unit cell lengths	605.740, 605.740, 466.710
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.000 - 3.400
R-factor	0.26
Structure solution method	Icosahedral averaging
Starting model (for MR)	Cryo-EM structure of the capsid at 20 Angstroms resolution
RMSD bond length	0.007
RMSD bond angle	26.382 *
Data reduction software	DENZO
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.000
High resolution limit [Å]	3.200	3.400 *
Rmerge	0.126
Total number of observations	1370632 *
Number of reflections	685316 *
Completeness [%]	50.0	54 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.8	300	Ammonium dihydrogen phosphate, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 300K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	ammonium phosphate	0.5 (M)