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. 2016 Oct 6;6:33357. doi: 10.1038/srep33357

Table 2. Data collection and refinement statistics (molecular replacement).

  XerDC-FtsKγ
Data collection
Space group P 65
Cell dimensions
a, b, c (Å) 83.44, 83.44, 88.66
 α, β, γ (°) 90, 90, 120
Resolution (Å) 56.02–2.30 (2.38–2.30)*
Rmerge 0.12 (1.66)
Rpim 0.04 (0.54)
CC(1/2) 1.00 (0.53)
II 13.8 (2.1)
Completeness (%) 100 (100)
Redundancy 11.0 (11.2)
Refinement
Resolution (Å) 36.13 - 2.3 (2.38–2.30)
No. reflections 15639 (1566)
Rwork/Rfree 0.191 (0.287)/0.229 (0.303)
CCwork 0.84 (0.65)
CCfree 0.85 (0.78)
CC* 0.94 (0.80)
No. atoms 1976
 Protein 1915
 Ligand/ion
 Water 61
B-factors Overall 67.5
 Protein 67.9
 Ligand/ion
 Water 52.6
R.M.S. deviations
 Bond lengths (Å) 0.01
 Bond angles (°) 1.16

Values in parentheses are for highest-resolution shell.