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. 2021 Jul 27;12(4):e00763-21. doi: 10.1128/mBio.00763-21

TABLE 2.

Model refinement and validation statisticsa

Rep (ssDNA) Rep (dsDNA)
Particles used for reconstruction 169,830 43,282
Box size 256 × 256 256 × 256
Pixel size 0.832 0.832
FSC resolution (Å)b 3.7 4.0
Global resolution (Å)c 3.8 4.4
B-factor sharpening (Å2)d −207.1 −250.0
CC (model to map fit) 80.8 75.2
 
Model composition
 Nonhydrogen atoms 17,553 18,067
 Residues
  DNA 6 24
  Protein 1,092 1,092
 B-factor avg (nucleotide) 58.53 157.81
 B-factor avg (protein) 65.21 81.50
Root mean square deviations
 Bond lengths (Å) 0.010 0.009
 Bond angles (°) 1.51 1.38
 Chirality (°) 0.06 0.06
 Planarity (°) 0.008 0.008
Validation
 Clashscore 4.58 4.65
 Protein validation
 MolProbity score 1.89 1.91
 EMringer score 2.85 2.29
 Ramachandran plot (%)
  Favored 98.53 98.53
  Allowed 1.47 1.47
  Outliers 0 0
 Rotamer outliers (%) 7.44 7.55
 PDB entry 7LAR 7LAS
 EMDB 23249 23250
a

The difference in FSC and global resolution (as determined by 3DFSC) indicates minimal anisotropy. The refinement statistics are indicative of a structure with appropriate geometry.

b

Fourier shell correlation reported by cryoSPARC V2 using the gold standard method at a correlation coefficient of 0.143.

c

Determined by 3DFSC.

d

The B-factor sharpening applied by cryoSPARC V2 during the postrefinement process.