Table 1 Data collection and refinement statistics (molecular replacement).

From: Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing

  Crystal 1 HEGA-10 (dehydrate) Crystal 2 HEGA-10 (hydrate) Crystal 3 NM
Data collection
 Space group C2 C2 C2221
Cell dimensions
a, b, c (Å) 117.07, 74.08, 107.93 111.13, 72.97, 101.78 86.5, 103.9, 184.52
α,β,γ (°) 90.0, 118.26, 90.0 90.0, 114.57, 90.0 90.0, 90.0, 90.0
 Resolution (Å) 50.0–3.49 (3.58–3.49)* 60.0–3.97 (4.14–3.97) 20.0–4.2 (4.3–4.2)
Rsym or Rmerge 4.8 (159.9) 13.9 (227.2) 8.7 (289.3)
II 22.98 (1.54) 7.3 (1.5) 7.18 (0.38)
 Completeness (%) 83.1 (25.6) 97.8 (86.0) 99.1 (99.6)
 Redundancy 11.1 (10.0) 8.8 (8.0) 3.7 (3.5)
Refinement
 Resolution (Å) 43.62–3.49 60.0–3.99 42–4.2
 No. of reflections 8747 5555 4801
Rwork/Rfree 27.1/28.5 27.2/32.1 27.1/30.3
No. of atoms
 Protein 2,717 2,734 2,717
 Ligand/ion 0 0 0
 Water 42 15 18
B-factors
 Protein 139.0 135.2 138.6
 Ligand/ion NA NA NA
 Water 74.1 135.1 138.6
Root mean square deviations
 Bond lengths (Å) 0.01 0.01 0.009
 Bond angles (degrees) 1.21 1.25 1.16
  1. HEGA-10, decanoyl-N-hydroxyethylglucamide; NA, not applicable; NM, n-nonyl-β-D-maltopyranoside.
  2. *Highest resolution shell is shown in parenthesis.