Table 1. Cryo-EM data collection, refinement and validation statistics.
| LmClpX1/2 dimer | LmClpXP1/2 EMD-10162, (PDB-6SFX, 6SFW) |
||
|---|---|---|---|
| Data collection and processing | |||
| Magnification | x112,807 | X112,807 | |
| Voltage (kV) | 300 | 300 | |
| Electron exposure (e–/Å2) | 114 | 114 | |
| Defocus range (μm) | 0.5 - -3.0 | -0.5 - -3.0 | |
| Pixel size (Å) | 1.1 | 1.1 | |
| Symmetry imposed | C1 | C1 | |
| Initial particle images (no.) | 273,300 | 613,322 | |
| Final particle images (no.) | 143,901 | 613,322 | |
| Map resolution (Å) | 13 | 4 | |
| FSC threshold | 0.143 | 0.143 | |
| Map resolution range (Å) | - | 3.2-10 | |
| Refinement | 6SFX 6SFW | ||
| Initial model used (PDB code) | - | 4RYF | - |
| Model resolution (Å) | - | 2.8, | - |
| FSC threshold | - | - | - |
| Model resolution range (Å) | - | - | - |
| Map sharpening B factor (Å2) | - | -214 | -240 |
| Model composition | |||
| Nonhydrogen atoms | - | 20196 | 15225 |
| Protein residues | - | 2602 | 1955 |
| Ligands | - | - | |
| B factors (Å2) | 100.8 | 187.87 | |
| Protein | - | - | |
| Ligand | - | - | |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.012 | 0.018 | |
| Bond angles (°) | 1.233 | 1.978 | |
| Validation | |||
| MolProbity score | - | 2.34 | 2.30 |
| Clashscore | - | 22.88 | 22.43 |
| Poor rotamers (%) | - | 0.18 | 0.2 |
| Ramachandran plot | |||
| Favored (%) | - | 92.04 | 92.9 |
| Allowed (%) | - | 7.65 | 6.4 |
| Disallowed (%) | - | 0.31 | 0.7 |