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. Author manuscript; available in PMC: 2021 May 1.
Published in final edited form as: FEBS J. 2019 Nov 19;287(9):1886–1898. doi: 10.1111/febs.15113

Table 1.

Data collection and refinement statistics.

Data collection Diamond i02
 Wavelength 0.9795
 Space group I222
 Molecules/a.u. 1
 Unit cell a, b, c (Å); 48.81, 69.99, 71.24
     α=β=γ (°) 90, 90, 90
 Resolution (Å)* 49.92–1.02 (1.04–1.02)
Rmerge (%) 3.8 (28.8)
Rpim (%)& 1.9 (23.1)
 No. of reflections
  (measured/unique)
242564/55708
 <II> 28.3 (2.8)
 Completeness (%) 89.4 (37)
 Redundancy 4.35
Refinement
 Resolution (Å) 49.92–1.02
 No. of reflections 53080/2642
  (refinement/ Rfree)
R / Rfree 12.10/15.00
 No. atoms
  Protein 1093
  Ligand/ion 51
  Water 220
 R.m.s. deviations from ideal
  Bond lengths (Å) 0.020
  Bond angles (°) 1.98
 Ramachandran plot
  Favored (%) 98.4
  Allowed (%) 1.6
 PDB code 6qaz
*

The highest resolution shell is shown in parentheses.

Rmerge = ∑hi | Ii–〈I〉 | / ∑hI Ii, where Ii is the observed intensity of the i-th measurement of reflection h, and 〈I〉 is the average intensity of that reflection obtained from multiple observations.

&

Defined in Weisse et al., 2001 [59].

R = ∑ ||Fo|–|Fc|| / ∑|Fo|, where Fo and Fc are the observed and calculated structure factors, respectively, calculated for all data. Rfree was defined in Brünger, 1992 [60].