5L1X
Structure of the Human Metapneumovirus Fusion Protein in the Postfusion Conformation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-07-24 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9793 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 128.720, 128.720, 572.790 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 37.019 - 3.300 |
R-factor | 0.223 |
Rwork | 0.221 |
R-free | 0.26970 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3rrr |
RMSD bond length | 0.008 |
RMSD bond angle | 1.123 |
Data reduction software | iMOSFLM |
Data scaling software | Aimless (0.5.12) |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 37.020 | 37.020 | 3.370 |
High resolution limit [Å] | 3.300 | 16.170 | 3.300 |
Rmerge | 0.216 | 0.053 | 1.015 |
Rmeas | 0.238 | ||
Rpim | 0.099 | ||
Total number of observations | 398399 | ||
Number of reflections | 73617 | ||
<I/σ(I)> | 5.2 | ||
Completeness [%] | 99.8 | 89.2 | 99.9 |
Redundancy | 5.4 | 4.1 | 5.6 |
CC(1/2) | 0.993 | 0.998 | 0.802 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 291 | 18.5% PEG3350, 11% MPD, 0.2 M lithium sulfate, 0.01 M nickel chloride, 0.1 M imidazole |