Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-03-23 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.978565 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 50.003, 84.322, 118.348 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.860 - 1.590 |
| R-factor | 0.2006 |
| Rwork | 0.199 |
| R-free | 0.23500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.040 |
| Data reduction software | autoPROC |
| Data scaling software | autoPROC |
| Phasing software | MOLREP |
| Refinement software | BUSTER (2.10.4) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.858 | 1.781 |
| High resolution limit [Å] | 1.610 | 1.610 |
| Rmerge | 0.261 | 1.800 |
| Number of reflections | 44967 | 2248 |
| <I/σ(I)> | 1.83 | |
| Completeness [%] | 94.2 | |
| Redundancy | 13.7 | |
| CC(1/2) | 0.997 | 0.690 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | IN CELL | 293 | over-expressed protein in cell |
