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. Author manuscript; available in PMC: 2021 Oct 2.
Published in final edited form as: J Mol Biol. 2020 Sep 6;432(21):5765–5783. doi: 10.1016/j.jmb.2020.08.026

Table 1.

Statistics on diffraction data and structure refinement of unliganded PDE6C GAFaba, b, c

Data collection
 Space group P65
 Unit cell (a = b, c, Å) 148.5, 148.5, 93.7
 Resolution (Å) 3.2
 Wavelength (Å) 1.0
 Unique reflections 16,737
 Redundancy 4.8 fold
 Completeness (%) 86.0 (87.7)a
 Average I/σ 6.2 (1.9)a
Rmerge 0.142 (0.712)a
Refinement
R-factor 0.207
R-free 0.308 (5.0%)b
 Resolution (Å) 50–3.2
  Bond (Å) 0.011
  Angle 1.65°
  Protein 72.5 (6251)c
Ramachandran plot
 Most favored 94.0
 Allowed 5.8
 Generally allowed 0.2
a

The numbers in parentheses are for the highest-resolution shell.

b

The percentage of reflections omitted for calculation of R-free.

c

The number of atoms in the crystallographic asymmetric unit.