6OAF
Sudan virus nucleoprotein core domain in complex with VP35 chaperoning peptide
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 | PIXEL |
Collection date | 2016-09-16 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 1.2819 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 126.840, 33.750, 101.860 |
Unit cell angles | 90.00, 101.46, 90.00 |
Refinement procedure
Resolution | 43.350 - 2.200 |
R-factor | 0.2136 |
Rwork | 0.212 |
R-free | 0.24810 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4ztg |
RMSD bond length | 0.003 |
RMSD bond angle | 0.564 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.610 | 2.300 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.084 | 1.361 |
Rpim | 0.049 | 0.922 |
Number of reflections | 22033 | |
<I/σ(I)> | 12.1 | |
Completeness [%] | 99.5 | |
Redundancy | 6.8 | |
CC(1/2) | 0.997 | 0.490 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8.5 | 293.15 | 20% PEG3350, 0.2 M potassium fluoride pH 8.5, 0.1 M bicine |