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

From: The cryo-EM structure of the bacterial flagellum cap complex suggests a molecular mechanism for filament elongation

 

FliDcj (EMDB-10210) (PDB: 6SIH)

Filament (EMDB-10244)

Data collection and processing

Microscope

Titan Krios

Tecnai Arctica

Magnification

36232

53000

Voltage (kV)

300

200

Camera

K2 Summit

Falcon III

Pixel size (Å)

1.38

2.03

Symmetry Imposed

D5 (full map), C5 (head map)

Helical (Rise: 7.25 Å, Twist: 65.4°)

Defocus range (µm)

−1.0 to −2.6

−0.8 to −2.0

Total dose (eÅ−2)

41

45

Number of micrographs

1223

100

Total particles used

55967

71828

Map Resolution (Å)

4.7 (full map) 5.0 (head domain)

8.6 (symmetrical) 27.2 (asymmetrical)

Refinement

Map sharpening B factor (Å2)

−285

 

Model composition

 Non-hydrogen atoms

37320

 

 Protein Residues

4880

 

B factors (Å−1)

 Protein

148

 

R.m.s. deviations

 Bond lengths (Å)

0.005

 

 Bond angles (°)

0.543

 

Validation

 MolProbity score

1.85

 

 Clashscore

8.36

 

 Poor rotamers (%)

0.00

 

Ramachandran plot

 Favored (%)

94.13

 

 Allowed (%)

5.87

 

 Disallowed (%)

0.00