4H5O
Crystal Structure of Rift Valley Fever Virus Nucleocapsid Protein Pentamer Bound to Single-stranded RNA
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 | CCD |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0332 |
| Spacegroup name | P 1 |
| Unit cell lengths | 79.810, 93.590, 124.780 |
| Unit cell angles | 101.70, 90.27, 114.18 |
Refinement procedure
| Resolution | 41.600 - 3.900 |
| R-factor | 0.229 |
| Rwork | 0.228 |
| R-free | 0.24840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3lyf |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.870 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.3.20) |
| Phasing software | PHASER |
| Refinement software | BUSTER-TNT (BUSTER 2.10.0) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 121.596 | 41.601 | 4.110 |
| High resolution limit [Å] | 3.900 | 12.330 | 3.900 |
| Rmerge | 0.210 | 0.463 | |
| Total number of observations | 1640 | 8356 | |
| Number of reflections | 28961 | ||
| <I/σ(I)> | 2.8 | 1.9 | 1 |
| Completeness [%] | 99.1 | 93.9 | 99.1 |
| Redundancy | 2 | 1.9 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 28% PEG3350, 280 mM ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
