Table 1 Cryo-EM data collection, 3D reconstruction and refinement statistics
From: Structural basis for enzymatic terminal C–H bond functionalization of alkanes
Data collection | |
Microscope | Titan Krios G3i |
Magnification | ×130,000 |
Stage type | Autoloader |
Voltage (kV) | 300 |
Detector | Gatan K3 |
Energy filter (eV) | 15 |
Acquisition mode | Super-resolution |
Physical pixel size (Å) | 0.666 |
Defocus range (µm) | 0.7–2.5 |
Electron exposure (e− Å−2) | 60 |
Reconstruction | |
Software | Relion v.3.08, CryoSPARC v.2.15 |
Particles picked (no.) | 2,950,051 |
Particles final (no.) | 46,953 |
Extraction box size (pixels) | 128 |
Rescaled box size (pixels) | 64 |
Final pixel size (Å) | 1.332 |
Symmetry imposed | C1 |
Map resolution (Å) | 2.76 |
FSC threshold | 0.143 |
Map resolution range (Å) | 341–2.72 |
Map sharpening B factor (Å2) | 66 |
Model refinement | |
Software | PHENIX |
Refinement algorithm | Real Space |
Clipped box size (pixels) | None |
Residues (no.) | 428 |
Iron (no.) | 3 |
Ligand (no.) | 1 |
R.m.s. deviations | |
Bond lengths (Å) | 0.004 |
Bond angles (°) | 0.573 |
Validation | |
MolProbity clashscore | 4.79 |
Rotamer outliers (%) | 0.0 |
Cβ deviations (%) | 0.0 |
Ramachandran plot | |
Favored (%) | 94.58 |
Allowed (%) | 5.42 |
Outliers (%) | 0 |
