Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-06-09 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.99988 |
| Spacegroup name | P 62 2 2 |
| Unit cell lengths | 90.968, 90.968, 338.333 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 41.200 - 2.920 |
| R-factor | 0.2059 |
| Rwork | 0.205 |
| R-free | 0.22040 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.950 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | BUSTER |
| Refinement software | BUSTER (2.11.7) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.200 | 3.170 |
| High resolution limit [Å] | 2.920 | 2.920 |
| Rmerge | 0.062 | 0.435 |
| Rmeas | 0.075 | 0.532 |
| Number of reflections | 18434 | 3935 |
| <I/σ(I)> | 13.4 | 2.6 |
| Completeness [%] | 97.0 | 98.3 |
| Redundancy | 2.77 | 2.82 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 293 | The purified protein was used in crystallisation trials employing both, a standard screen with approximately 1200 different conditions, as well as crystallisation conditions identified using literature data. Conditions initially obtained have been optimised using standard strategies, systematically varying parameters critically influencing crystallisation, such as temperature, protein concentration, drop ratio, and others. These conditions were also refined by systematically varying pH or precipitant concentrations. |
