Table 2 Cryo-EM data collection, refinement, and validation statistics

From: Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB

 

YaxAB (20-mer)

(EMDB-3885)

(PDB-6EL1)

Data collection and processing

 

  Magnification

59,000

  Voltage (kV)

300

  Electron exposure (e–/Å2)

60

  Defocus range (μm)

1.1–2.5

  Pixel size (Å)

1.106

  Symmetry imposed

C10

  Initial particle images (no.)

178,149

  Final particle images (no.)

24,822

  Map resolution (Å)

6.1

   FSC threshold

0.143

  Map resolution range (Å)

4.8–7.0

Refinement

 

  Initial model used (PDB code)

6EK7, 6EK8

  Model resolution (Å)

6.1

   FSC threshold

0.143

  Model resolution range (Å)

4.8–7.0

  Map sharpening B-factor (Å2)

−331

 Model composition

 

   Protein residues

6830

 B-factors (Å2)

 

   Protein

322

 R.m.s. deviations

 

   Bond lengths (Å)

0.005

   Bond angles (°)

0.93

 Validation

 

   MolProbity score

1.87

   Clashscore

7.4

   Poor rotamers (%)

0.5

 Ramachandran plot

 

   Favored (%)

92.5

   Allowed (%)

7.5

   Disallowed (%)

0

  1. The Yersinia YaxAB system is a pore-forming toxin of so far unknown structure. Here authors present X-ray and cryo-EM to structures of individual subunits and of the YaxAB pore complex, and find that YaxA binds to membranes first and recruits YaxB for subsequent oligomerization