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

From: Capture, mutual inhibition and release mechanism for aPKC–Par6 and its multisite polarity substrate Lgl

 

aPKCι–Par6α–Llgl1 (EMD-18877), (PDB 8R3Y)

Data collection and processing

Magnification

165,000

Voltage (kV)

300

Electron exposure (e per Å2)

48.1

Defocus range (μm)

−1.5 to −3.5

Pixel size (Å)

0.82

Symmetry imposed

C1

Initial particle images (no.)

1,069,057

Final particle images (no.)

121,194

Map resolution (Å)

3.6

 FSC threshold

0.143

Map resolution range (Å)

10.6-2.0

Refinement

Initial model used (PDB code)

6N8Q, 8R3X, 1NF3

Model resolution (Å)

3.58 (masked)

 FSC threshold

0.5

Map sharpening B factor (Å2)

67.0

Model composition

 

 Nonhydrogen atoms

10,132

 Protein residues

1,374

 Ligands

1

B factors (Å2)

 

 Protein

52.95

 Ligand

51.30

Root-mean-square deviations

 

 Bond lengths (Å)

0.024

 Bond angles (°)

3.170

Validation

 

 MolProbity score

2.27

 Clashscore

0

 Poor rotamers (%)

3%

Ramachandran plot

 

 Favored (%)

92%

 Allowed (%)

8%

 Disallowed (%)

0%

  1. FSC, Fourier shell correlation.