4H5Q
Crystal Structure of Rift Valley Fever Virus Nucleocapsid Protein Hexamer Bound to Single-stranded DNA
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 64 2 2 |
| Unit cell lengths | 108.640, 108.640, 261.290 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 53.660 - 2.700 |
| R-factor | 0.1911 |
| Rwork | 0.189 |
| R-free | 0.22990 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3lyf |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.060 |
| 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] | 94.085 | 53.658 | 2.850 |
| High resolution limit [Å] | 2.700 | 8.540 | 2.700 |
| Rmerge | 0.031 | 0.779 | |
| Total number of observations | 3587 | 15490 | |
| Number of reflections | 25771 | ||
| <I/σ(I)> | 10 | 16.8 | 1 |
| Completeness [%] | 99.6 | 95.5 | 98.5 |
| Redundancy | 4.4 | 4 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 15% PEG3350, 350 mM sodium chloride, 100 mM Bis-Tris, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |






