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 |