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

From: The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems

#1 Candida albicans γ-TuSC (EMD-11835) (PDB-7ANZ)

Data collection and processing

Dataset 1

Dataset 2

Magnification

81,000

81,000

Voltage (kV)

300

300

Electron exposure (e–/Å2)

40

40

Defocus range (μm)

−2 to −3

−2 to −3

Pixel size (Å)

1.07

1.07

Initial particle images (no.)

309,744

1,502,064

Final particle images (no.)

45,351

228,975

Merged set of particles

274,326

Map resolution (Å)

3.6

FSC threshold

0.143

Model resolution range (Å)

3.3-4.7

Refinement

  

 Initial model used (PDB code)

Homology models derived from human GCP4 (3RIP) and γ-tubulin (1Z5W)

 Model resolution (Å)

3.6

4.2

  FSC threshold

0.143

0.5

 Model resolution range (Å)

3.5-4.3

 Map sharpening B factor (Å2)

−60.0

 Model composition

 

  Non-hydrogen atoms

16,759

  Protein residues

2041

  Ligands

0

 B factors (Å2)

 

  Protein

5.71/82.31/35.50

  Ligand

−/−/−

 R.m.s. deviations

 

  Bond lengths (Å)

0.003

  Bond angles (°)

0.786

 Validation

 

  MolProbity score

1.66

  Clashscore

4.57

  Poor rotamers (%)

0.31

 Ramachandran plot

 

  Favored (%)

93.36

  Allowed (%)

6.49

  Disallowed (%)

0.15