8GPH
Crystal structure of protease 3C (C160A mutant) from Seneca Valley Virus
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 | 2021-08-17 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9788 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 47.253, 69.441, 75.705 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.979 - 1.608 |
R-factor | 0.1759 |
Rwork | 0.175 |
R-free | 0.19310 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6l0t |
RMSD bond length | 0.006 |
RMSD bond angle | 0.875 |
Data reduction software | autoPROC |
Data scaling software | autoPROC |
Phasing software | PHASER |
Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.690 |
High resolution limit [Å] | 1.608 | 1.610 |
Rmerge | 0.055 | 0.546 |
Rmeas | 0.059 | 0.619 |
Rpim | 0.043 | 0.445 |
Number of reflections | 32177 | 4383 |
<I/σ(I)> | 22.2 | 2.7 |
Completeness [%] | 97.0 | 92.6 |
Redundancy | 12 | 8 |
CC(1/2) | 0.999 | 0.858 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 4% (w/v) PEG 8000, 0.1 M HEPES (pH 7.5) |