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

From: Molecular basis for the interaction between Saccharomyces cerevisiae Rtt103 and the Rat1-Rai1 complex

 

Saccharomyces cerevisiae Rat1-Rai1-Rtt103 complex

Data collection and processing

Magnification

105,000

Voltage (kV)

300

Electron exposure (e2)

49.3

Defocus range (μm)

–0.6 to –2

Pixel size (Å)

0.413

Symmetry imposed

C1

Image stacks (no.)

6718

Initial particles images (no.)

3,614,995

Final particle images (no.)

552,608

Map resolution (Å)

2.85

FSC threshold

0.143

Map sharpening B-factor (Å2)

–123

Refinement

Number of protein residues

1115

Number of metal ions

1

Number of atoms

8975

R.m.s. deviations

 

Bond lengths (Å)

0.004

Bond angles (°)

0.536

PDB validation

 

Clash score

6

Poor rotamers (%)

0

Ramachandran plot

 

Favored (%)

98.5

Allowed (%)

1.5

Disallowed (%)

0.0