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 | 2019-09-28 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.953731 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 82.951, 159.687, 209.245 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.440 - 2.500 |
| Rwork | 0.199 |
| R-free | 0.22230 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6wet |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.373 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.487 | 2.540 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rpim | 0.041 | 0.567 |
| Number of reflections | 96772 | 4657 |
| <I/σ(I)> | 15.1 | 1.3 |
| Completeness [%] | 99.9 | |
| Redundancy | 26.1 | |
| CC(1/2) | 0.999 | 0.650 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 281 | 7.5 mg/mL protein against 19-22% PEG4000, 240-270 mM trilithium/triammonium/tripotassium citrate |
