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

From: Cryo-EM structures of the translocational binary toxin complex CDTa-bound CDTb-pore from Clostridioides difficile

 

Di-heptamer

Long

Short

Folded

Unfolded

EMDB ID

EMD-33188

EMD-32043

EMD-32041

EMD-34136

EMD-34137

PDB ID

7VNN

7VNJ

7YVQ

7YVS

Data collection and processing

 Magnification

81,000

 Voltage (kV)

300

 Electron exposure (e-2)

50

 Defocus range (μm)

−0.8 to −2.0

 Pixel size (Å)

0.88

 Symmetry imposed

C1

 Initial particle images (no.)

2,608,418

 Final particle images (no.)

102,116

83,061

167,398

24,981

100,912

 Map resolution (Å)

3.19

2.64

2.56

3.18

2.80

 FSC threshold

0.143

0.143

0.143

0.143

0.143

 Map sharpening B factor (Å2)

−67.1

−32.3

−36.4

−56.1

−70.9

Refinement

 Model resolution (Å)

3.2

2.8

3.4

3.0

 FSC threshold

0.5

0.5

0.5

0.5

Model composition

 Non-hydrogen atoms

38,823

30,661

30,742

30,593

 Protein residues

4863

3856

3874

3856

 Ligands

21

21

21

21

B factors (Å2)

 Protein

61.64

93.72

90.02

78.04

 Ligand

45.36

77.75

73.97

63.43

R.m.s deviations

 Bond lengths (Å)

0.004

0.004

0.005

0.005

 Bond angles (Å)

0.949

0.956

0.977

0.990

Validation

 MolProbity score

1.74

1.65

1.76

1.68

 Clashscore

6.31

5.58

6.34

6.12

 Poor rotamers (%)

0.37

0.40

0.75

0.98

Ramachandran plot

 Favored (%)

94.27

95.01

93.78

95.09

 Allowed (%)

5.73

4.99

6.22

4.91

 Disallowed (%)

0.00

0.00

0.00

0.00

  1. Table containing details of cryo-EM data collection, processing, and refinement including relevant statistics for all maps and models generated in this study.