Table 1 Summary of cryo-EM data collection, processing and analysis.

From: Plant-expressed virus-like particles reveal the intricate maturation process of a eukaryotic virus

Data set

Procapsid

Capsid

Data collection and processing

 Microscope

Titan Krios

Titan Krios

 Detector (mode)

Falcon III (integrating)

Falcon III (integrating)

 Magnification

75,000 ×

75,000 ×

 Magnified pixel size (Å)

1.065

1.065

 Voltage (kV)

300

300

 Total dose (e2)

72.0

79.5

 Defocus range (μm)

−0.7 to −2.7

−0.8 to −3.0

 Movies collected

8554

2788

 Particle images

5426

21,395

 Symmetry imposed

Icosahedral (I1)

Icosahedral (I1)

 FSC threshold

0.143

0.143

 Map resolution (Å)

6.63

2.72

 Map resolution range (Å)

5.66–13.33

2.64–3.77

Refinement

 Initial model used (PDB code)

7ANM

1OHF

 Map sharpening B factor (Å2)

−452.2

−125.0

 Model composition (ASU)

Chains A, B, C, D

Chains A, B, C, D

 Non-hydrogen atoms

17,464

17,518

 Protein residues

2288

2290

R.m.s. deviations

 Bond lengths (Å)

0.005

0.006

 Bond angles (°)

1.02

1.04

Validation

 EMRinger score

N/Aa

5.1

 Molprobity score

2.93

1.59

 Clashscore

22.45

4.06

 Poor rotamers (%)

9.68

2.08

 Ramachandran plot:

  Favoured (%)

95.2

97.1

  Allowed (%)

4.8

2.9

  Disallowed (%)

0.0

0.0

  Ramachandran Z-score

1.02 ± 0.02

1.36 ± 0.02

 Fit to map (CCmask)

0.74

0.88

Accession codes

 EMPIAR (dataset)

10555

10560

 EMDB (maps)

11911

11830

 PDB (model)

7ATA

7ANM

  1. aThe EMRinger score uses the density around side-chains to evaluate the fit of the protein backbone. At a resolution of 6.6 Å there is no discernible side-chain density and thus the EMRinger score is meaningless.