Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-02-06 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9655 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 33.430, 48.890, 35.670 |
| Unit cell angles | 90.00, 103.53, 90.00 |
Refinement procedure
| Resolution | 34.680 - 1.800 |
| R-factor | 0.16529 |
| Rwork | 0.163 |
| R-free | 0.21750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.508 |
| 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] | 48.880 | 1.850 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Number of reflections | 10206 | 639 |
| <I/σ(I)> | 9.25 | |
| Completeness [%] | 97.5 | |
| Redundancy | 3.15 | |
| CC(1/2) | 0.996 | 0.624 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | Crystallization technique: sitting drop of 150 nL (ratio 2:1, protein:precipitant). Protein stock: 20 mg / mL into 150 mM NaCl, 25 mM TRIS 8, 4 mM CaCl2. 200 nL Precipitant: PEG Suite Qiagen H12 (0.18 M tri-Ammonium citrate, 20 %(w/v) PEG 3350). |
