8YM1
Structure of SADS-CoV Virus Nucleocapsid Protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL10U2 |
| Synchrotron site | SSRF |
| Beamline | BL10U2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-01-02 |
| Detector | DECTRIS EIGER2 S 9M |
| Wavelength(s) | 0.9791 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 48.417, 95.897, 103.998 |
| Unit cell angles | 90.00, 96.25, 90.00 |
Refinement procedure
| Resolution | 51.740 - 1.900 |
| R-factor | 0.18998 |
| Rwork | 0.189 |
| R-free | 0.22563 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | AlphaFold |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.834 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0425) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 95.900 | 1.940 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.777 | |
| Number of reflections | 73150 | 4547 |
| <I/σ(I)> | 11.1 | |
| Completeness [%] | 98.4 | |
| Redundancy | 6.3 | |
| CC(1/2) | 0.997 | 0.787 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289 | 0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate at pH 4.6, and 36% PEG 4000 |
