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 | 2020-02-14 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 61.497, 73.650, 132.172 |
| Unit cell angles | 90.00, 95.67, 90.00 |
Refinement procedure
| Resolution | 39.763 - 1.470 |
| Rwork | 0.160 |
| R-free | 0.18470 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3kro |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.844 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MoRDa |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.840 | 1.490 |
| High resolution limit [Å] | 1.470 | 1.470 |
| Rmerge | 0.085 | 0.805 |
| Rpim | 0.035 | 0.334 |
| Number of reflections | 98723 | 4443 |
| <I/σ(I)> | 10.5 | |
| Completeness [%] | 98.2 | 89.6 |
| Redundancy | 6.9 | 6.6 |
| CC(1/2) | 0.999 | 0.885 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | Droplets were 200 nL protein at 10 mg/mL plus 200 nL reservoir, 0.2 M MgCl2 and 20 %(w/v) PEG 3350. |
