9J4U
Structural basis for recognition of SARS-CoV-2 conserved nucleocapside epitopes by dominant T cell receptors
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL02U1 |
Synchrotron site | SSRF |
Beamline | BL02U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2024-06-09 |
Detector | DECTRIS EIGER2 S 9M |
Wavelength(s) | 0.9792 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 54.757, 148.273, 64.210 |
Unit cell angles | 90.00, 109.15, 90.00 |
Refinement procedure
Resolution | 60.660 - 2.170 |
R-factor | 0.1952 |
Rwork | 0.193 |
R-free | 0.23910 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 0.922 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | REFMAC |
Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 60.700 | 2.250 |
High resolution limit [Å] | 2.170 | 2.170 |
Number of reflections | 51116 | 5086 |
<I/σ(I)> | 16.1 | |
Completeness [%] | 99.9 | |
Redundancy | 4.8 | |
CC(1/2) | 0.999 | 0.799 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | 0.2 M potassium sodium tartrate tetrahydrate, and 20% (w/v) PEG 3350 |