Table 2 Cryo-EM data collection, refinement, and validation statistics.

From: Structural and biochemical rationale for Beta variant protein booster vaccine broad cross-neutralization of SARS-CoV-2

 

Ancestral

Beta

Data collection and processing

 Grid type

UltraAuFoil 200 mesh R1.2/1.3

UltraAuFoil 200 mesh R1.2/1.3

 Plunge freezer

Vitrobot

Vitrobot

 Magnification

240,000

240,000

 Voltage (kV)

200

200

 Camera

Falcom4

Falcom4

 Electron exposure (e/Å^2)

62

62

 Defocus range (µm)

(− 0.8 to − 2.2)

(− 0.8 to − 2.2)

 Pixel size (Å)

0.58

0.58

 Micrographs

19,667

10,494

 No. of fractions

55

55

 Symmetry imposed

none

none

 Initial particles imaged (no.)

2,618,182

2,186,869

 Initial particles imaged (no.)

349,329

262,895

 Map resolution (Å)#

2.85

2.75

 FSC treshold

0.143

0.143

Refinement*

 Model resolution (Å)#

3.1

3

  FSC treshold

0.5

0.5

 Model resolution range (Å)

  Map sharpening B factor (Å^2)

93.9

79.5

 Model composition

  Non-hydrogen atoms

20,801

19,482

  Protein residues

2659

2454

  Ligands

35

29

 B factors (Å^2)

  Protein residues (mean)

76.81

71.77

  Ligands (mean)

100.06

90.52

 R.m.s deviations

  Bond lenghts (Å)

0.002

0.003

  Bond angles (º)

0.455

0.478

 Validation

  MolProbity score

1.4

1.54

  Clashscore

4.77

4.69

 Ramachandran plot

  Favored (%)

97.18

95.73

  Allowed (%)

2.82

4.27

  Disallowed

0

0

  1. #resolution from Cryosparc v3.2.0.
  2. *Using comprehensive validation in Phenix (1.20.1–4487).