2I9F
Structure of the equine arterivirus nucleocapsid protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 200 |
| Detector technology | CCD |
| Collection date | 2006-05-18 |
| Detector | MAR CCD 165 mm |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 68.230, 73.230, 138.960 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.940 - 2.000 |
| R-factor | 0.21866 |
| Rwork | 0.217 |
| R-free | 0.24753 |
| Structure solution method | SAD |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.623 |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | DM |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.940 | 2.060 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.079 | 0.525 |
| Number of reflections | 25482 | |
| <I/σ(I)> | 28.9 | 7 |
| Completeness [%] | 99.1 | 98.2 |
| Redundancy | 19.5 | 19.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 311 | 0.1M sodium phosphate, 25% PEG 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 311K |
