Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | NUCLEAR REACTOR |
| Source details | FRM II BEAMLINE BIODIFF |
| Synchrotron site | FRM II |
| Beamline | BIODIFF |
| Temperature [K] | 294 |
| Detector technology | IMAGE PLATE |
| Collection date | 2020-02-02 |
| Detector | BIODIFF |
| Wavelength(s) | 3.1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.542, 78.316, 47.893 |
| Unit cell angles | 90.00, 97.36, 90.00 |
Refinement procedure
| Resolution | 24.950 - 2.095 |
| Rwork | 0.178 |
| R-free | 0.24250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.028 |
| RMSD bond angle | 0.950 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.180 |
| High resolution limit [Å] | 2.095 | 2.095 |
| Rmeas | 0.168 | 0.473 |
| Rpim | 0.106 | 0.334 |
| Number of reflections | 13758 | 886 |
| <I/σ(I)> | 4.6 | |
| Completeness [%] | 80.8 | 52.4 |
| Redundancy | 1.9 | |
| CC(1/2) | 0.971 | 0.716 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH MODE | 294 | Purified protein and crystallisation buffer were mixed at a 1:1 ratio. Crystallisation buffer was 20% PEG 3350, 200 mM sodium thiocyanate. |
