4V9E
Crystal Structure of Rift Valley Fever Virus Nucleocapsid Protein Hexamer Bound to Single-stranded RNA.
This is a non-PDB format compatible entry.
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 | 91.660, 173.330, 172.900 |
| Unit cell angles | 119.95, 99.34, 90.12 |
Refinement procedure
| Resolution | 57.420 - 3.400 |
| R-factor | 0.2254 |
| Rwork | 0.225 |
| R-free | 0.23990 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3lyf |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.850 |
| 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] | 149.472 | 57.417 | 3.580 |
| High resolution limit [Å] | 3.400 | 10.750 | 3.400 |
| Rmerge | 0.050 | 0.513 | |
| Total number of observations | 7343 | 31220 | |
| Number of reflections | 117933 | ||
| <I/σ(I)> | 4 | 3.5 | 1.3 |
| Completeness [%] | 94.7 | 95.6 | 92.3 |
| Redundancy | 1.9 | 1.9 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 24% PEG3350, 350 mM ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
