7QTO
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 | 2019-11-29 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.95372 |
Spacegroup name | I 1 2 1 |
Unit cell lengths | 56.909, 57.009, 61.598 |
Unit cell angles | 90.00, 117.37, 90.00 |
Refinement procedure
Resolution | 30.740 - 3.500 |
R-factor | 0.2437 |
Rwork | 0.242 |
R-free | 0.26570 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5vwc |
RMSD bond length | 0.002 |
RMSD bond angle | 0.551 |
Data reduction software | DIALS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.15.2_3472) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.740 | 3.630 |
High resolution limit [Å] | 3.500 | 3.500 |
Rmerge | 0.130 | 0.210 |
Number of reflections | 4238 | 429 |
<I/σ(I)> | 6.5 | |
Completeness [%] | 97.9 | |
Redundancy | 3.1 | |
CC(1/2) | 0.970 | 0.930 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 0.2M Ammonium sulfate, 30% w/v PEG 4000 |