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. Author manuscript; available in PMC: 2023 Jan 1.
Published in final edited form as: Proteins. 2022 Feb 28;90(7):1457–1467. doi: 10.1002/prot.26326

Table 1.

Crystal data collection and structure refinement statistics

RsgI9S1C-CTD
Data collection
Space group P 1 21 1
Cell dimensions
  a, b, c (Å) 63.63, 78.06, 81.21
  α, β, γ (°) 90.00, 112.98, 90.00
Resolution (Å) 74.77-2.00 (2.05-2.00)
Wavelength (Å) 0.97903
Total observations 246720 (17477)
Unique reflections 48797 (3594)
Rmerge (%) 4.9 (61.8)
I / σI 16.51 (2.60)
CC1/2 99.9 (83.9)
Completeness (%) 98.4 (98.2)
Multiplicity 5.1 (4.9)
Wilson B-factor (Å2) 40.84
Refinement
Resolution (Å) 74.77-2.00
No. of reflections 48797
Rwork / Rfree (%) 19.7/21.9
No. atoms 5058
  Protein 4788
  Ligand/ion 78
  Water 192
B-factors (Å2) (all atoms) 51.5
  Protein 51.4
  Ligand/ion 64.1
  Water 48.1
R.m.s. deviations
  Bond lengths (Å) 0.012
  Bond angles (°) 1.49
Ramachandran favored (%) 99.03
Ramachandran allowed (%) 0.97
Ramachandran outliers (%) 0.00
PDB ID 7SJY

Values in parentheses are for the highest-resolution shell.