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 | 2020-11-14 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 60.720, 73.261, 68.817 |
| Unit cell angles | 90.00, 109.17, 90.00 |
Refinement procedure
| Resolution | 45.160 - 1.840 |
| Rwork | 0.188 |
| R-free | 0.23210 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7mxz |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.575 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.160 | 1.880 |
| High resolution limit [Å] | 1.840 | 1.840 |
| Rmerge | 0.100 | 1.367 |
| Rpim | 0.042 | 0.587 |
| Number of reflections | 24629 | 1295 |
| <I/σ(I)> | 9.4 | 1.3 |
| Completeness [%] | 99.0 | 85.7 |
| Redundancy | 6.7 | |
| CC(1/2) | 0.998 | 0.574 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | Protein was at 10 mg/mL and the drops were 200 nL plus 200 nL with the reservoir being 22.5% PEG 3350, 0.3M MgCl2, 0.1M Na-HEPES pH 6.55 |
