8FWL
Crystal structure of Australian bat lyssavirus nucleoprotein in complex with phosphoprotein chaperone
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-06-26 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 1 2 1 |
| Unit cell lengths | 82.373, 35.503, 89.091 |
| Unit cell angles | 90.00, 92.63, 90.00 |
Refinement procedure
| Resolution | 29.670 - 2.190 |
| R-factor | 0.1611 |
| Rwork | 0.159 |
| R-free | 0.19250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.546 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.670 | 2.260 |
| High resolution limit [Å] | 2.190 | 2.190 |
| Rmerge | 0.076 | 0.464 |
| Rmeas | 0.538 | |
| Rpim | 0.268 | |
| Number of reflections | 26863 | 2185 |
| <I/σ(I)> | 10.4 | 3.3 |
| Completeness [%] | 99.5 | |
| Redundancy | 3.8 | |
| CC(1/2) | 0.997 | 0.866 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 0.12M Alcohol mix (0.2M 1,6-Hexanediol; 0.2M 1-Butanol; 0.2M 1,2-Propanediol; 0.2M 2-Propanol; 0.2M 1,4-Butanediol; 0.2M 1,3-Propanediol), 1.0M Tris (base); BICINE,60% Precipitant Mix (40% v/v PEG 500* MME; 20 % w/v PEG 20000) |






