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) |