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

From: Structural and biochemical characterisation of the Providencia stuartii arginine decarboxylase shows distinct polymerisation and regulation

 

Adc stack

Adc decamer

 

EMDB 13466 PDB 7PK6

EMDB 13261 PDB 7P9B

Data collection and processing

Magnification

215,000

215,000

Voltage (kV)

300

300

Electron exposure (e−/Å2)

40.0

40.0

Defocus range (μm)

−0.5–−2.5

−0.5–−2.5

Pixel size (Å)

0.65

0.65

Symmetry imposed

D5

D5

Initial particle images (no.)

438,429

303,475

Final particle images (no.)

268,579

46,854

Map resolution (Å)

2.15

2.44

 FSC threshold

0.143

0.143

Map resolution range (Å)

2.07–3.56

2.42–3.29

Refinement

Initial model used (PDB code)

2VYC

PDB 7PK6

Model resolution (Å) (masked)

2.42

2.56

 FSC threshold

0.5

0.5

Map sharpening B factor (Å2)

−74 Å−2

−75 Å−2

Model composition

 Non-hydrogen atoms

120,580

60,290

 Protein residues

15,100

7550

 Ligands

0

0

B factors (Å−2)

 Protein

23.00

47.08

R.m.s. deviations

 Bond lengths (Å)

0.006

0.009

 Bond angles (°)

0.649

1.127

Validation

 MolProbity score

1.47

1.51

 Clashscore

4.28

7.23

 Poor rotamers (%)

2.22

0.93

Ramachandran plot

 Favoured (%)

98.00

97.47

 Allowed (%)

2.00

2.53

 Outliers (%)

0.00

0.00