1H2D
Ebola virus matrix protein VP40 N-terminal domain in complex with RNA (Low-resolution VP40[31-212] variant).
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Spacegroup name | P 62 2 2 |
Unit cell lengths | 79.610, 79.610, 239.180 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 59.800 * - 2.600 |
R-factor | 0.306 |
Rwork | 0.305 |
R-free | 0.32900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1h2c |
RMSD bond length | 0.009 * |
RMSD bond angle | 1.420 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | BEAST |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 60.000 | |
High resolution limit [Å] | 2.600 | |
Rmerge | 0.085 | 0.406 * |
Total number of observations | 63464 * | |
Number of reflections | 14356 * | |
<I/σ(I)> | 4.5 | |
Completeness [%] | 97.8 | 86 * |
Redundancy | 4.4 | 3.6 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 * | 1 UL OF PROTEIN (13 MG/ML) AND 1 UL OF WELL SOLUTION (100 MM NA-ACETATE PH4.6, 35 % MPD, 4 % GLYCEROL).HANGING DROP., pH 4.60 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | HEPES | 100 (mM) | pH7.5 |
3 | 1 | reservoir | 1.5 (M) | ||
4 | 1 | reservoir | MPD | 15 (%) |