5WB0
Crystal structure of human metapneumovirus fusion glycoprotein stabilized in the prefusion state
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 17-ID-1 |
Synchrotron site | NSLS-II |
Beamline | 17-ID-1 |
Temperature [K] | 77 |
Detector technology | PIXEL |
Collection date | 2017-04-07 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 0.919774 |
Spacegroup name | I 21 3 |
Unit cell lengths | 177.700, 177.700, 177.700 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 51.298 - 2.601 |
R-factor | 0.1719 |
Rwork | 0.170 |
R-free | 0.20690 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5l1x 5c69 |
RMSD bond length | 0.003 |
RMSD bond angle | 0.561 |
Data reduction software | MOSFLM |
Data scaling software | Aimless (0.5.31) |
Phasing software | PHASER |
Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 51.300 | 51.300 | 2.720 |
High resolution limit [Å] | 2.600 | 9.010 | 2.600 |
Rmerge | 0.165 | 0.051 | 1.422 |
Rmeas | 0.174 | 0.054 | 1.496 |
Rpim | 0.055 | 0.017 | 0.465 |
Total number of observations | 284021 | 7320 | 35787 |
Number of reflections | 28796 | ||
<I/σ(I)> | 11.2 | 31.5 | 1.9 |
Completeness [%] | 100.0 | 99.5 | 100 |
Redundancy | 9.9 | 9.9 | 10.3 |
CC(1/2) | 0.997 | 0.998 | 0.546 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 0.82 M LiSO4, 0.41 M (NH4)2SO4, 0.1 M Na3-citrate pH 5.5 |