3EBJ

Crystal structure of an avian influenza virus protein

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2008-04-20
Detector	SBC-2
Wavelength(s)	0.9798
Spacegroup name	P 1
Unit cell lengths	51.049, 59.825, 67.165
Unit cell angles	96.55, 96.82, 109.51

Refinement procedure

Resolution	50.000 - 2.200
R-factor	0.234
Rwork	0.231
R-free	0.25200
Structure solution method	SAD
RMSD bond length	0.009
RMSD bond angle	1.399
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MLPHARE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.300
High resolution limit [Å]	2.200	2.200
Rmerge	0.067	0.490
Number of reflections	31554
Completeness [%]	98.0	95
Redundancy		2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	291	25% PEG8000 (native crystals) or 20% PEG3350, pH6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
1	VAPOR DIFFUSION, HANGING DROP	6.5	291	25% PEG8000 (native crystals) or 20% PEG3350, pH6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K