3CSY

Crystal structure of the trimeric prefusion Ebola virus glycoprotein in complex with a neutralizing antibody from a human survivor

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	100
Detector technology	CCD
Collection date	2006-08-23
Detector	ADSC QUANTUM 315
Wavelength(s)	0.98030
Spacegroup name	H 3 2
Unit cell lengths	273.710, 273.710, 409.430
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	48.369 - 3.400
R-factor	0.263
Rwork	0.261
R-free	0.30200
Structure solution method	phase combination of model phases from an independently solved Fab KZ52 and Fab KZ52 selenium anomalous signal
RMSD bond length	0.011
RMSD bond angle	1.100
Data reduction software	d*TREK
Data scaling software	d*TREK (9.6D)
Phasing software	PHASER
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.370	48.370	3.520
High resolution limit [Å]	3.400	7.320	3.400
Rmerge	0.142	0.047	0.568
Total number of observations		76813	54223
Number of reflections	151305
<I/σ(I)>	6.2	18.5	1.7
Completeness [%]	96.2	96.8	94.7
Redundancy	4.14	4.9	3.58

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	295	8.5% (w/v) PEG 10,000, 0.1 M Tris-HCl pH 8.5, 0.4 M sodium acetate, 10% (v/v) PEG 200, VAPOR DIFFUSION, HANGING DROP, temperature 295K