Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | FREE ELECTRON LASER |
| Source details | SACLA BEAMLINE BL2 |
| Synchrotron site | SACLA |
| Beamline | BL2 |
| Temperature [K] | 298 |
| Detector technology | CCD |
| Collection date | 2019-06-26 |
| Detector | MPCCD |
| Wavelength(s) | 1.127 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.079, 78.290, 47.389 |
| Unit cell angles | 90.00, 97.36, 90.00 |
Refinement procedure
| Resolution | 30.096 - 1.600 |
| Rwork | 0.190 |
| R-free | 0.20800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.760 |
| Data reduction software | DIALS |
| Data scaling software | DIALS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.100 | 1.628 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Number of reflections | 37266 | 1877 |
| <I/σ(I)> | 12.1 | 4.6 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 618.7 | 274.5 |
| CC(1/2) | 0.990 | 0.910 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH MODE | 294 | Purified protein, diluted crystal seeds, and crystallisation buffer were mixed at a 1:1.5:1.5 ratio. Crystallisation buffer was 25% PEG 3350, 200 mM sodium thiocyanate. Crystal seed stock was diluted 1:20 in 25% PEG 3350. |
