8W3Q
Crystal structure of prefusion-stabilized hMPV F protein UFCM1-P2-iSS
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 | 2023-09-02 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.97 |
Spacegroup name | I 21 3 |
Unit cell lengths | 185.745, 185.745, 185.745 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.640 - 5.990 |
R-factor | 0.23 |
Rwork | 0.224 |
R-free | 0.35460 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.018 |
RMSD bond angle | 2.380 |
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] | 49.640 | 6.215 |
High resolution limit [Å] | 5.990 | 5.990 |
Number of reflections | 2793 | 278 |
<I/σ(I)> | 22.42 | |
Completeness [%] | 99.6 | |
Redundancy | 38.2 | |
CC(1/2) | 0.999 | 0.728 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.4M potassium dihydrogen phosphate, 1.2M sodium dihydrogen phosphate, 0.1M phosphate-citrate pH4.37 |