8E15
A computationally stabilized hMPV F protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-04-21 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1 |
Spacegroup name | I 21 3 |
Unit cell lengths | 178.191, 178.191, 178.191 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.620 - 2.410 |
R-factor | 0.2058 |
Rwork | 0.204 |
R-free | 0.24870 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5wb0 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.017 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.620 | 2.496 |
High resolution limit [Å] | 2.410 | 2.410 |
Number of reflections | 36363 | 3606 |
<I/σ(I)> | 9.18 | 0.78 |
Completeness [%] | 99.9 | 99.86 |
Redundancy | 2 | 2 |
CC(1/2) | 0.999 | 0.593 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 298 | 0.1 M Sodium acetate trihydrate pH 4.6, 2.0 M Sodium formate |