5FMO
Crystal structure and proteomics analysis of empty virus like particles of Cowpea mosaic virus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-04-03 |
Detector | DECTRIS PILATUS3 6M |
Spacegroup name | I 41 |
Unit cell lengths | 655.970, 655.970, 571.451 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.300 |
R-factor | 0.359 |
Rwork | 0.359 |
R-free | 0.36200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ny7 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.566 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.420 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.290 | 0.450 |
Number of reflections | 3192363 | |
<I/σ(I)> | 3.7 | 1.7 |
Completeness [%] | 60.3 | 49.6 |
Redundancy | 2.3 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.8 | 0.1M SODIUM ACETATE PH 4.7 3-4%(W/V)PEG 3350 0.3M AMMONIUM SULFATE 5% GLYCEROL |