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. 2015 Jul 24;25(9):1043–1059. doi: 10.1038/cr.2015.86

Table 1. Summary of diffraction data and structure refinement statistics.

Diffraction data
Wavelength (Å) 0.9794
Space group P41212
Cell parameters
a, b, c (Å) 48.12, 48.12, 223.38
Resolution (Å) 50.0-2.40 (2.49-2.40)a
Observed reflections 67 134
Unique reflections (I/σ(I) > 0) 11 033
Average redundancy 6.2 (6.3)
Average I/σ(I) 18.7 (4.6)
Completeness (%) 99.7 (99.7)
Rmerge (%) 7.6 (52.0)
Refinement and structure model
Reflections (Fo≥0σ(Fo))
Working set 10 503
Test set 528
Rwork/Rfree (%) 17.1/22.0
No. of protein atoms 1 939
No. of solvent atoms 58
Average B factor (Å2)
All atoms 50.0
Protein atoms 50.1
Solvent atoms 47.2
RMS deviation
Bond lengths (Å) 0.008
Bond angles (°) 1.09
Ramachandran plot (%)b
Most favored regions 98.0
Other allowed regions 2.0
Outliers 0.0

aNumbers in parentheses represent the highest resolution shell.

bStatistics of the Ramachandran plot was analyzed using MolProbity.