Table 1 Cryo-EM data collection/processing

From: Molecular mechanism of setron-mediated inhibition of full-length 5-HT3A receptor

 

5-HT3A-granisetron (EMDB-0469; PDB-6NP0)

Data collection and processing

  Magnification

×130,000

  Voltage (kV)

300

  Electron exposure (e2)

40

  Defocus range (μm)

−1.0 to −2.5

  Pixel size (Å)

0.532

  Symmetry imposed

C5

  Initial particle images (no.)

243,290

  Final particle images (no.)

46, 757

  Map resolution (Å)

2.92

    FSC threshold

0.143

Refinement

  Initial model used (PDB code)

6BE1

  Map sharpening B-factor (Å2)

−50

  Model composition

    Non-hydrogen atoms

16,891

    Protein residues

16,300

    Ligands

591

  B factors (Å2)

    Protein

111.12

    Ligand

117.85

  RMS deviations

    Bond lengths (Å)

0.008

    Bond angles (°)

1.072

  Validation

    MolProbity score

1.51 (95th percentile)

    Clashscore

3.63 (97th percentile)

    Poor rotamers (%)

0.55

  Ramachandran plot

    Favored (%)

94.83

    Allowed (%)

5.17

    Disallowed (%)

0.00

  1. Cryo-EM cryogenic electron microscopy, FSC Fourier shell coefficient, RMS root mean square, PDB Protein Data Bank code