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. 2011 Sep 29;286(47):40608–40613. doi: 10.1074/jbc.M111.257550

TABLE 1.

Data collection and refinement statistics

Data collection
    Space group P3221
    Unit cell dimension (Å) a = b = 92.8, c = 90.8
    Resolution range (Å) 40.0-2.65
    Unique reflections 13,522 (847)a
    Average redundancy 10.7 (8.2)a
    Rsym (%)b 10.2 (59.2)a
    I/σ(I) 23.7 (2.9)a
    Completeness (%) 99.9 (98.1)a

Refinement statistics
    Refinement resolution (Å) 36.8-2.65
    Rcryst (%)c 24.8 (28.5)d
    Rfree (%) 27.6 (30.4)d
    Protein atoms 2,036
    Waters and ligands 49×H2O, 1×PEG, 9×NAG, 3×MAN, 1×FUCe
    Root mean square deviation from ideal values
        Bond length (Å) 0.007
        Bond angle (°) 1.12
    Mean B-factor (Å2) 84.3
    Wilson plot B-factor (Å2) 87.2
    Ramachandran statistics
        Most favored region (%) 95.3
        Additionally allowed (%) 4.7

a Values are for the highest resolution shell in data collection (2.71-2.65 Å).

b Rsym = ΣhΣi|Ii(hkl) − 〈I(hkl)〉|/ΣhΣiIi(hkl).

c Rcryst = Σ‖Fo| − |Fc‖/Σ|Fo|, calculated from working data set. Rfree was calculated from 7.08% of data randomly chosen not to be included in refinement.

d Values are for the highest resolution shell in structure refinement (2.86-2.65 Å).

e NAG (N-acetyl glucosamine), MAN (mannose), FUC (fucose).