1RD8

Crystal Structure of the 1918 Human H1 Hemagglutinin Precursor (HA0)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-2
Synchrotron site	SSRL
Beamline	BL9-2
Temperature [K]	100
Detector technology	CCD
Collection date	2003-02-21
Detector	ADSC QUANTUM 315
Wavelength(s)	0.984
Spacegroup name	C 1 2 1
Unit cell lengths	190.529, 109.953, 136.238
Unit cell angles	90.00, 108.63, 90.00

Refinement procedure

Resolution	49.400 * - 3.000
R-factor	0.27128
Rwork	0.270
R-free	0.29600 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.019
RMSD bond angle	1.850 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.400 *	3.070
High resolution limit [Å]	3.000	3.000
Rmerge	0.146 *	0.520 *
Total number of observations	125868 *
Number of reflections	51346	3368 *
<I/σ(I)>	7.6	1.4
Completeness [%]	96.4	95.1 *
Redundancy	2.5	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	294	sodium phosphate, potassium phosphate, sodium citrate, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 294K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	reservoir	sodium dihydrogen phosphate	1.68 (M)
3	1	reservoir	dipotassium hydrogen phosphate	0.32 (M)
4	1	reservoir	phosphate citrate	0.1 (M)	pH5.5