Table 1

Crystallographic data and refinement statistics

Statistics
Data statistics 
    Resolution, Å 50.0-2.15 
    Space group P212121 
    Cell constants, Å a = 54.5, b = 146.6, c = 229.0 
    Molecules/asymmetric unit 
    Total observations 877 794 
    Unique reflections 82 662 
    Mean redundancy 6.7 
    *Rsym, % 6.4 (33.1) 
    Completeness, % 94.8 (83.4) 
    Mean I/s 29.5 (4.2) 
Refinement statistics 
    Resolution, Å 50.0-2.4 
    Rcryst, % 21.4 
    Rfree, % 24.2 
    Average B factor, Å 2 33.6 
    No. of model atoms 10 676 
    No. of solvent sites 260 
RMS deviations from ideals 
    Bond length, Å 0.008 
    Bond angles, deg 1.08 
Statistics
Data statistics 
    Resolution, Å 50.0-2.15 
    Space group P212121 
    Cell constants, Å a = 54.5, b = 146.6, c = 229.0 
    Molecules/asymmetric unit 
    Total observations 877 794 
    Unique reflections 82 662 
    Mean redundancy 6.7 
    *Rsym, % 6.4 (33.1) 
    Completeness, % 94.8 (83.4) 
    Mean I/s 29.5 (4.2) 
Refinement statistics 
    Resolution, Å 50.0-2.4 
    Rcryst, % 21.4 
    Rfree, % 24.2 
    Average B factor, Å 2 33.6 
    No. of model atoms 10 676 
    No. of solvent sites 260 
RMS deviations from ideals 
    Bond length, Å 0.008 
    Bond angles, deg 1.08 

The atomic coordinates have been deposited in the Protein Data Bank23  under the access code 3E1I (rfD-BbD432A+GH).

*

Rsym = Σ|I − 〈I〉|, where I is the observed intensity and 〈I〉 is the average intensity of multiple symmetry-related observations of that reflection.

Rcryst = Σ(|Fobs| − |Fcalc|)/Σ|Fobs|, where Fobs and Fcalc are the observed and calculated structure factors, respectively.

Rfree is the R-factor based on the 5% of the data withheld from structural refinement.

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