1EBO
CRYSTAL STRUCTURE OF THE EBOLA VIRUS MEMBRANE-FUSION SUBUNIT, GP2, FROM THE ENVELOPE GLYCOPROTEIN ECTODOMAIN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ELLIOTT GX-13 |
Temperature [K] | 290 |
Detector technology | IMAGE PLATE |
Collection date | 1998-08-15 |
Detector | MARRESEARCH |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 171.702, 32.691, 168.863 |
Unit cell angles | 90.00, 119.23, 90.00 |
Refinement procedure
Resolution | 20.000 - 3.000 |
Rwork | 0.239 |
R-free | 0.25600 |
Structure solution method | SIR |
RMSD bond length | 0.016 |
RMSD bond angle | 1.700 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CCP4 |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.090 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.083 * | 0.290 * |
Total number of observations | 87380 * | |
Number of reflections | 17123 | |
Completeness [%] | 99.3 | 99.2 |
Redundancy | 5.1 | 3.07 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 9.3 * | 0.02ml of protein solution was mixed with 0.01ml of reservoir solution * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | |
3 | 1 | reservoir | Tris-HCl | 100 (mM) | |
4 | 1 | reservoir | PEG4000 | 30-34 (%) | |
5 | 1 | reservoir | ammonium sulfate | 220 (mM) | |
6 | 1 | reservoir | dioxane | 1.0 (%) |