Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-3 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-3 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-06-30 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.9677 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 75.512, 143.173, 335.372 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 132.024 - 3.325 |
| Rwork | 0.204 |
| R-free | 0.26750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4wsb |
| RMSD bond length | 0.003 |
| RMSD bond angle | 1.217 |
| Data reduction software | XDS |
| Data scaling software | autoPROC |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0257) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 132.024 | 3.463 |
| High resolution limit [Å] | 3.325 | 3.325 |
| Rmerge | 0.190 | 2.298 |
| Rmeas | 0.199 | 2.388 |
| Rpim | 0.057 | |
| Number of reflections | 50439 | 2523 |
| <I/σ(I)> | 10.7 | 1.5 |
| Completeness [%] | 92.7 | 42.2 |
| Redundancy | 11.6 | 13.3 |
| CC(1/2) | 0.997 | 0.500 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 281 | Protein at about 9 mg/ml 0.1 M Tris pH 7.0, 8-13% PEG 8K, 0.2 M MgCl2, 0.1 M guanidine hydrochloride |
