1PP1
Crystal structure of the Borna Disease Virus Nucleoprotein
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X31 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X31 |
| Temperature [K] | 100 |
| Detector technology | AREA DETECTOR |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9793, 0.802, 0.9787 |
| Spacegroup name | I 4 |
| Unit cell lengths | 100.261, 100.261, 103.340 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.230 - 1.900 |
| R-factor | 0.15484 |
| Rwork | 0.153 |
| R-free | 0.18220 |
| Structure solution method | MAD |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.414 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.1.19) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Number of reflections | 38615 | |
| <I/σ(I)> | 17.07 | 1.5 |
| Completeness [%] | 95.3 | 75.1 |
| Redundancy | 3.19 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 9 * | 20 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 8 (mg/ml) | |
| 2 | 1 | reservoir | PEG550 MME | 15 (%) | |
| 3 | 1 | reservoir | 0.1 (M) | ||
| 4 | 1 | reservoir | dithiothreitol | 2-5 (mM) | |
| 5 | 1 | reservoir | Bicine | 0.1 (M) | pH9.0 |
