Table 1 Cryo-EM data collection, refinement, and validation statistics.

From: Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion

 

SOD1 fibril (EMD-32227, PDB 7VZF)

Data collection and processing

 

Magnification

130,000

Voltage (kV)

300

Camera

K2 summit (Titan Krios)

Frame exposure time (s)

0.16

Movie frames (n)

40

Electron exposure (e2)

60

Defocus range (μm)

−2.0 to −1.2

Pixel size (Å)

1.04

Symmetry imposed

C1

Box size (pixel)

320

Inter-box distance (Å)

33.3

Micrographs collected (n)

2931

Segments extracted (n)

288,744

Segments after Class2D (n)

147,525

Segments after Class3D (n)

70,067

Map resolution (Å)

2.95

 FSC threshold

0.143

Map resolution range (Å)

2.30–5.01

Refinement

 

Initial model used

De novo

Model resolution (Å)

2.95

 FSC threshold

0.143

Model resolution range (Å)

2.95

Map sharpening B factor (Å2)

−77.93

Model composition

 

 Nonhydrogen atoms

2,628

 Protein residues

363

 Ligands

0

B factors (Å2)

 

 Protein

70.90

R.m.s. deviations

 

 Bond lengths (Å)

0.009

 Bond angles (°)

1.060

Validation

 

MolProbity score

2.86

Clashscore

37.29

Poor rotamers (%)

0

Ramachandran plot

 

 Favored (%)

73.50

 Allowed (%)

26.50

 Disallowed (%)

0