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. Author manuscript; available in PMC: 2014 Nov 1.
Published in final edited form as: Nat Struct Mol Biol. 2014 Apr 20;21(5):456–463. doi: 10.1038/nsmb.2814

Table 2.

Crystallographic statistics for the A399C A432CHg mutant.

CLC-ec1 Cys-less A399C A432CHg
Data collection
Space group C2
Cell dimensions
    a, b, c (Å) 233.5, 94.5, 170.6
    α, β, γ (°) α, β,γ (°) 90, 131.75, 90
Resolution (Å) 43.56 (3.52) *)*
Rsym or Rmerge (%) 11.5 (52.2))*
I / σ/σI 6.57 (1.90))*
Completeness (%) 98.76 (97.88))*
Redundancy 3.3 (3.2))*
Refinement
Resolution (Å) 43.56-3.52
No. reflections 34345
Rwork / Rfree 0.22/0.26
No. atoms
    Protein 13225
    Ligand/ion 4
    Water 0
B factors
    Protein 91.5
    Ligand/ion 90.9
r.m.s. deviations
    Bond lengths (Å) 0.002
    Bond angles (°) 0.620
*

Values in parentheses are forrefer to the outermost shell. * Data was collected from a single crystal. *Values in parentheses are for highest-resolution shell.