Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID30B |
| Synchrotron site | ESRF |
| Beamline | ID30B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-05-10 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 1.77 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 78.552, 96.682, 105.579 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.333 - 1.800 |
| Rwork | 0.209 |
| R-free | 0.24320 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1r56 reconstructed dimer |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.451 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 71.322 | 1.826 |
| High resolution limit [Å] | 1.723 | 1.723 |
| Rmerge | 0.057 | 0.542 |
| Rmeas | 0.062 | 0.630 |
| Rpim | 0.017 | 0.260 |
| Number of reflections | 72278 | 3531 |
| <I/σ(I)> | 22.8 | 2 |
| Completeness [%] | 93.8 | 56.5 |
| Redundancy | 11.4 | 5.3 |
| CC(1/2) | 0.999 | 0.802 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH MODE | 8 | 291 | 20 microliter of protein (15 mg/ml) mixed with 20 microliter of solution: Buffer Tris 0.05M (chloride free) + 4% PEG 4000. |
