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. 2023 Jan 20;79(Pt 2):140–153. doi: 10.1107/S2059798322012190

Table 1. Cryo-EM data collection, processing and refinement of the AAV4 structure.

Data collection
 Magnification 165000×
 Voltage (V) 300
 Electron exposure (e− Å−2) 47
 Defocus range −3.9 to 1.0
 Pixel size (pre-refinement) (Å) 0.253
 Pixel size (post-refinement) (Å) 0.254
Data processing
 Motion correction RELION 3.1.1
 CTF estimation CTFFIND4.1
 Symmetry imposed I1
 Initial particle images 85449
 Final particle images 85411
 Map resolution (Å) 2.21
 FSC threshold 0.143
Refinement
 Protein atoms per asymmetric unit (mean B factor, Å2) 4333 (21.9)
 Solvation 219 H2O/2 Mg2+
 R.m.s.d. from ideal, bond lengths (Å) 0.11
 R.m.s.d. from ideal, bond angles (°) 1.3
 Ramachandran outliers 1
 Cross-correlation (model–map; grid points within 2.2 Å of atoms) 0.871
 Envelope correction/equivalent overall B factor (for optimal fitting of model to sharpened map) (Å2) −4.3/−17.2
 Resolution from model–map refinement (RSRef d 0.5) 2.3