Table 1 Cryo-EM data collection and modeling statistics.

From: Cryo-EM structure-based selection of computed ligand poses enables design of MTA-synergic PRMT5 inhibitors of better potency

 

PRMT5:MEP50:11-2 F

PRMT5:MEP50

Data collection and processing

  Magnification

105,000

105,000

  Voltage (kV)

300

300

  Electron exposure (e2)

40

40

  Defocus range (μm)

−0.75 to −3.0

−0.75 to −3.0

  Pixel size (Å)

0.66

0.66

  Symmetry imposed

D2

D2

  Initial number of particle images (no.)

866,240

235,210

  Final number of particle images (no.)

207,392

101,707

  Map sharpening B factor (Å2)

−68

−79.7

  Overall map resolution (Å)

3.14

3.17

  FSC threshold

0.143

0.143

Refinement

  Initial model used (PDB code)

Apo PRMT map

Generated in Relion3.0

  FSC model (0/0.143/0.5) Å

3.1/3.2/3.4

2.9/3.2/3.6

Model composition (per asymmetric unit)

  Chains

2

2

  Non-hydrogen atoms

7384

7265

  Protein residues

932

925

  Ligands

2

0

  B factors (Å2)  (min/max/mean)

24.99/75.31/47.74

61.67/137.13/86.91

R.M.S. deviations

  Bond angles (°)

0.566

0.645

  Bond distances (Å)

0.005

0.007

Validation

  MolProbity score

0.78

1.05

  Clash score

0.69

0.89

  Poor rotamers (%)

0.00

0.00

Ramachandran plot

  Favored (%)

97.73

97.58

  Allowed (%)

2.16

1.87

  Outliers (%)

0.11

0.55

 EMringer Score

3.02

2.84