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 |