6L0T
Crystal structure of senecavirus A 3C protease
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL18U1 |
| Synchrotron site | SSRF |
| Beamline | BL18U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-03-16 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.97853 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.910, 57.600, 74.780 |
| Unit cell angles | 90.00, 100.26, 90.00 |
Refinement procedure
| Resolution | 27.570 - 1.900 |
| R-factor | 0.1761 |
| Rwork | 0.174 |
| R-free | 0.20630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2bhg |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.827 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (5.8.0253) |
| Phasing software | PHASER (3.25) |
| Refinement software | PHENIX (1.16_3549) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 27.570 | 1.950 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.115 | 0.167 |
| Number of reflections | 32921 | 4744 |
| <I/σ(I)> | 11.6 | |
| Completeness [%] | 99.9 | |
| Redundancy | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | 20% PEG 3350, 0.2 M Lithium chloride, 0.1M HEPES pH 7.5 |
