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. 2017 Jun 26;7:4218. doi: 10.1038/s41598-017-04441-x

Table 1.

Data collection and refinement statistics for FLNb16-17 crystal structure.

FLNb16-17a
Data collection
Space group P321
Cell dimensions
 a, b, c (Å) 80.62, 80.62, 118.02
 α, β, γ (°) 90, 90, 120
Resolution (Å) 118–2.49 (2.55–2.49)b
R sym 11.1 (66.1)
I/σI 12.8 (3.1)
Completeness (%) 99.7 (96.2)
Redundancy 12.4 (6.9)
Refinement
Resolution (Å) 12.4 (6.9)
No. reflections 15 238/802
R work/R free (%) 19.6/23.8
No. atoms
 Protein 2389
 Ligand/ion 0
 Water 11
B-factors (Å2)
 Protein 65.9
 Ligand/ion 0
 Water 53.8
R.m.s. deviations
 Bond lengths (Å) 0.01
 Bond angles (°) 1.62

aDiffraction data from a single crystal were used.

bValues in parentheses are for highest-resolution shell.