8FAH
Crystal structure of SARS-CoV-2 receptor binding domain in complex with SARS-CoV-2 reactive human antibody CR3022
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-03-09 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9792 |
Spacegroup name | P 41 2 2 |
Unit cell lengths | 151.176, 151.176, 192.928 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.980 - 4.220 |
R-factor | 0.2481 |
Rwork | 0.246 |
R-free | 0.28620 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond angle | 6.132 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 4.350 |
High resolution limit [Å] | 4.200 | 4.200 |
Number of reflections | 13814 | 800 |
<I/σ(I)> | 5.57 | |
Completeness [%] | 82.2 | |
Redundancy | 6.1 | |
CC(1/2) | 0.980 | 0.470 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 291 | 1M Succinic acid, 0.1M HEPES pH 7.0 and 2% PEG MME2000 |