7QTU
Structural biology of the NS1 avian influenza protein subversion on the Scribble cell polarity module
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-10-18 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.95372 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 77.836, 77.716, 64.752 |
Unit cell angles | 90.00, 94.16, 90.00 |
Refinement procedure
Resolution | 42.940 - 2.840 |
Rwork | 0.252 |
R-free | 0.29600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5vwi |
RMSD bond length | 0.004 |
RMSD bond angle | 0.757 |
Data reduction software | DIALS |
Data scaling software | Aimless |
Phasing software | PHASER (1.15.2-3472-000) |
Refinement software | PHENIX (1.15.2_3472) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 42.940 | 2.990 |
High resolution limit [Å] | 2.840 | 2.840 |
Rmerge | 0.069 | 0.370 |
Number of reflections | 8916 | 864 |
<I/σ(I)> | 9.6 | |
Completeness [%] | 96.9 | |
Redundancy | 3 | |
CC(1/2) | 0.990 | 0.750 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 0.1M Sodium Cacodylate pH4.2, 40% MPD |