6A9S
The crystal structure of vaccinia virus A26 (residues 1-397)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE TPS 05A |
| Synchrotron site | NSRRC |
| Beamline | TPS 05A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-05-23 |
| Detector | RAYONIX MX300-HS |
| Wavelength(s) | 0.97907 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.380, 80.718, 53.812 |
| Unit cell angles | 90.00, 113.80, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.180 |
| R-factor | 0.10773 |
| Rwork | 0.107 |
| R-free | 0.13002 |
| Structure solution method | SAD |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.532 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SHELXCD |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.220 |
| High resolution limit [Å] | 1.180 | 1.180 |
| Rmerge | 0.083 | 0.413 |
| Number of reflections | 114858 | 10993 |
| <I/σ(I)> | 13.7 | 2.2 |
| Completeness [%] | 99.4 | 95.2 |
| Redundancy | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 298 | 0.2 M sodium acetate trihydrate, 0.1 M Tris pH 8.5, 30 % w/v PEG 4000 |
