Table 1.

Data Collection, Phasing, and Refinement Statistics

NativeSe (λ1)Se (λ2)Se (λ3)
Diffraction Data
    Unit cell (Å)a = 117.3, b = 117.3, c = 255.3a = 117.75, b = 117.75, c = 255.82
    Wavelength (Å)0.97970.97924 (peak)0.97939 (edge)0.97563 (remote)
    Resolution (Å)2.853.13.13.1
    Space groupI41I4122I4122I4122
    No. of reflections117,97152,41652,51952,339
    No. of unique reflections38,53727,58027,64927,543
    Completeness96.2 (97.9)88.8 (91.0)88.6 (90.9)88.6 (90.9)
    Multiplicity3.1 (3.0)1.91.91.9
    R-sym (%)a6.9 (43)13.5 (79.8)13.9 (79.8)13.1 (76.2)
    I/σ(I)15.1 (2.2)7.1 (1.6)7.1 (1.6)7.6 (1.7)
Phasing
    Refined f′ (e-)−8.56−10.3−5.34
    Refined f″ (e-)5.062.51.13
    Mean figure of merit0.36
    No. of Se sites10
Structure Refinement
    Rfactor (%)b20.2
    Rfree (%)24.4
    No. of protein atoms7312
    No. of solvent atoms176
    No. of ligand atoms90
    RMS deviation of bond lengths (Å)0.007
    RMS deviation of bond angles (°)1.12
    RMS deviation of dihedral angles (°)9.35
    Average B factor (Å2)62.3
  • The numbers in parentheses indicate the value in the outer resolution shell. Rfree was calculated using 5% of reflections that were kept apart from the refinement during the whole process. RMS, root mean square.

  • a R-sym =Embedded Image.

  • b R-factor = Embedded Image.