4H5P
Crystal Structure of Rift Valley Fever Virus Nucleocapsid Protein Tetramer 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 | C 1 2 1 |
| Unit cell lengths | 77.640, 193.180, 77.420 |
| Unit cell angles | 90.00, 108.89, 90.00 |
Refinement procedure
| Resolution | 31.480 - 2.150 |
| R-factor | 0.1822 |
| Rwork | 0.180 |
| R-free | 0.21860 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3lyf |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.930 |
| 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] | 96.590 | 48.423 | 2.270 |
| High resolution limit [Å] | 2.150 | 6.800 | 2.150 |
| Rmerge | 0.045 | 0.584 | |
| Total number of observations | 7092 | 21896 | |
| Number of reflections | 55733 | ||
| <I/σ(I)> | 9.3 | 6.6 | 1.3 |
| Completeness [%] | 95.5 | 99.1 | 77.9 |
| Redundancy | 3.7 | 3.8 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 18% PEG3350, 350 mM sodium chloride, 100 mM Bis-Tris, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |






