8W3G
Crystal structure of prefusion-stabilized RSV F protein UFCR1(1TD0)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL12-1 |
Synchrotron site | SSRL |
Beamline | BL12-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-01-19 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.97 |
Spacegroup name | P 41 3 2 |
Unit cell lengths | 168.824, 168.824, 168.824 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 26.690 - 2.280 |
R-factor | 0.2247 |
Rwork | 0.223 |
R-free | 0.25520 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.483 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 26.690 | 2.362 |
High resolution limit [Å] | 2.280 | 2.280 |
Number of reflections | 37868 | 3611 |
<I/σ(I)> | 12.6 | |
Completeness [%] | 99.4 | |
Redundancy | 21.7 | |
CC(1/2) | 0.999 | 0.785 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2 M tri-Ammonium citrate, 12% PEG 3350 |