5FHC

Crystal Structure of Protective Human Antibodies 100 and 114 in Complex with Ebola Virus Fusion Glycoprotein (GP)

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	2014-10-24
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9792
Spacegroup name	H 3 2
Unit cell lengths	169.670, 169.670, 376.990
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	47.848 - 6.704
R-factor	0.2648
Rwork	0.260
R-free	0.34340
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.219
Data reduction software	MOSFLM
Data scaling software	Aimless (0.5.2)
Phasing software	PHASER
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	47.850	47.850	7.490
High resolution limit [Å]	6.700	14.990	6.700
Rmerge	0.301	0.071	1.678
Rpim	0.106	0.027	0.580
Total number of observations	35041	2938	10356
Number of reflections	3952
<I/σ(I)>	8.9	20.9	2.1
Completeness [%]	99.7	96.9	100
Redundancy	8.9	7.8	9.4
CC(1/2)	0.987	0.997	0.383

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	Ternary complex of Ebola virus GP (mucin-like domain deleted) with 114 and 100 at 2.9mg/ml, 13.4% PEG 8000, 6.7% isopropanol, 0.2M ammonium sulfate, 0.1M HEPES pH 7.5, 0.01M GSH-GSSG (L-Glutathione reduced-L-Glutathione oxidized)