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 | 2019-08-03 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.953731 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 83.111, 158.885, 209.832 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.400 - 2.600 |
| Rwork | 0.210 |
| R-free | 0.24420 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4b56 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.370 |
| 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] | 44.423 | 2.650 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rpim | 0.053 | 0.916 |
| Number of reflections | 86202 | 4500 |
| <I/σ(I)> | 12.9 | 1 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 26.1 | 14.5 |
| CC(1/2) | 0.998 | 0.539 |
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 |
