6AE5
Crystals structure of Classical swine fever virus NS5B (residues 1-672, Y471A mutant, form 1)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL19U1 |
Synchrotron site | SSRF |
Beamline | BL19U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-07-07 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.9785 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 160.653, 160.653, 55.647 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.743 - 2.754 |
R-factor | 0.1833 |
Rwork | 0.181 |
R-free | 0.23260 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2cjq |
RMSD bond length | 0.008 |
RMSD bond angle | 0.882 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.850 |
High resolution limit [Å] | 2.750 | 5.920 | 2.750 |
Rmerge | 0.118 | 0.078 | 0.456 |
Rmeas | 0.123 | 0.082 | 0.477 |
Rpim | 0.034 | 0.024 | 0.136 |
Number of reflections | 19483 | 2127 | 1908 |
<I/σ(I)> | 5.4 | ||
Completeness [%] | 100.0 | 99.8 | 100 |
Redundancy | 12.8 | 11.6 | 12.2 |
CC(1/2) | 0.995 | 0.966 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 289 | Polypropylene glycol 400 |