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

From: RhoA allosterically activates phospholipase Cε via its EF hands

EMDB: EMD-43927, EMD-43928

PDB: 9AX5

EMPIAR: EMPIAR-12069

Data collection

 Grids

Copper Quantifoil

 Vitrification method

FEI Vitrobot

 Microscope

FEI Titan Krios

 Magnification

81000

 Voltage (kV)

300

 Detector

GATAN K3 (6k × 4k)

 Electron exposure (e2)

57.8

 Number of frames

40

 Defocus range (mM)

0.6–2.0

 Pixel Size (Å)

0.527

Data processing

 Number of micrographs

6378

 Initial particle images (no.)

1,329,298

 Final particle images (no.)

209,463

 Symmetry

C1

 Map resolution (Å)

3.3

  FSC threshold

0.143

Refinement

 Map sharpening B factor (Å2)

133.2

 Map CC

0.80

 Model composition

 

  Non-hydrogen atoms

8544

  Protein residues

1065

  Ligands

3

 B factor (Å2; min/max/mean)

 

  Protein

20.13/162.65/57.21

  Ligand

27.98/138.95/134.91

 R.m.s. deviations

 

  Bond lengths (Å)

0.004

  Bond angles (°)

0.924

 Validation

 

  MolProbity score

1.60

  Clashscore

6.17

  Rotamer outliers (%)

1.05

  CaBLAM outliers (%)

1.45

 Ramachandran plot

 

  Favored (%)

96

  Allowed (%)

4

  Outliers (%)

0