4B3V
Crystal structure of the Rubella virus glycoprotein E1 in its post-fusion form crystallized in presence of 20mM of Calcium Acetate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 1 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-07-02 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 121.272, 126.163, 129.375 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.990 - 1.980 |
R-factor | 0.1854 |
Rwork | 0.185 |
R-free | 0.19790 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4adi |
RMSD bond length | 0.007 |
RMSD bond angle | 0.940 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | BUSTER (2.11.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.720 | 2.080 |
High resolution limit [Å] | 1.980 | 1.980 |
Rmerge | 0.080 | 0.500 |
Number of reflections | 135009 | |
<I/σ(I)> | 9.1 | 2 |
Completeness [%] | 97.1 | 81.5 |
Redundancy | 3.4 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 1-6% PEG 4K, 100 MM NAHEPES PH 8, 25% GLYCEROL, 20 MM CA(OAC)2 |