8W3I
Crystal structure of prefusion-stabilized RSV F protein UFCR1-L2
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 | 2022-04-27 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.97 |
Spacegroup name | P 41 3 2 |
Unit cell lengths | 168.999, 168.999, 168.999 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.790 - 2.300 |
R-factor | 0.2418 |
Rwork | 0.240 |
R-free | 0.27220 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.521 |
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] | 48.790 | 2.383 |
High resolution limit [Å] | 2.300 | 2.301 |
Number of reflections | 37127 | 3638 |
<I/σ(I)> | 11.93 | |
Completeness [%] | 99.8 | |
Redundancy | 20.9 | |
CC(1/2) | 0.998 | 0.845 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2 M tri-Sodium citrate, 18% PEG 3350 |