Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-06-19 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.976 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 60.909, 66.050, 107.277 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.780 - 1.610 |
| R-factor | 0.1734 |
| Rwork | 0.172 |
| R-free | 0.21000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ccl |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.140 |
| Data reduction software | XDS (b. 20180126) |
| Data scaling software | Aimless (0.7.1) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0131) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 56.240 | 1.670 |
| High resolution limit [Å] | 1.610 | 1.610 |
| Rmerge | 0.067 | 1.528 |
| Rmeas | 0.075 | 1.714 |
| Rpim | 0.033 | 0.765 |
| Number of reflections | 56743 | 5473 |
| <I/σ(I)> | 12.3 | |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 5.1 | 4.8 |
| CC(1/2) | 0.999 | 0.466 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.25 | 293 | Protein: 50 mM Tris, 150 mM NaCl, 1 mM (S)-diperodon, 10% DMSO, pH 8.0; reservoir: 100 mM Tris, 50 mM magnesium acetate, 11% PEG3350, pH 8.25 |
