Table 1 Data processing details, refinement, and validation statistics

From: Structural characteristics of alpha-fetoprotein, including N-glycosylation, metal ion and fatty acid binding sites

 

AFP (EMD-37997, PDB: 8X1N)

Data collection and processing

Magnification

165,000×

Voltage (kV)

300

Electron exposure (e-/Å2)

50

Defocus range (µm)

1.0–1.6

Pixel size (Å)

0.526

Symmetry imposed

C1

Micrographs

10,849

Initial particle images (no.)

739,577

Final particle images (no.)

144,221

Resolution offinal map [Å]

3.31

FSC threshold

0.143

B-factor applied [Å2]

−149.8

Refinement

Model composition

Non-hydrogen atoms

4763

Protein residues

591

R.m.s deviations

Bond lengths (Å)

0.003

Bond angles (°)

0.549

Validation

MolProbity score

1.15

Clashscore

2.85

Poor rotamers (%)

0.00

Ramachandran plot

Favored (%)

97.62

Allowed (%)

2.38

Disallowed (%)

0.00