Table I.

Data collection and refinement statistics

Data collection statistics

Temperature (K) 100 
x-ray source NSLS, Beamline X25 
Detector ADSC Q315 
Space group I4132 
Cell dimensions (Å) 345.2, 345.2, 345.2 
Resolution (Å) 50.0-3.40 
Total no. of observations 680267 
No. of unique observations 48105 (6919) 
Multiplicity 14.1 
Data completeness (%) 100.0 (100.0) 
I/σI 16.2 (3.0) 
RPIM (%) 4.6 (26.5) 
Refinement statistics  
Nonhydrogen atoms  
    Protein 10174 
    Water 
Resolution (Å) 50 – 3.4 
Rfactor (%) 24.8 
Rfree (%) 27.9 
r.m.s.d from ideality  
    Bond lengths (Å) 0.007 
    Bond angles (°) 1.53 
    Dihedrals 26.59 
    Impropers 0.963 
Ramachandran plot  
    Most favored 78.2 
    Allowed 20.0 
    Generous 1.0 
    Unfavored 0.8 
B-factors (Å2 
    Average per residue 110 
Data collection statistics

Temperature (K) 100 
x-ray source NSLS, Beamline X25 
Detector ADSC Q315 
Space group I4132 
Cell dimensions (Å) 345.2, 345.2, 345.2 
Resolution (Å) 50.0-3.40 
Total no. of observations 680267 
No. of unique observations 48105 (6919) 
Multiplicity 14.1 
Data completeness (%) 100.0 (100.0) 
I/σI 16.2 (3.0) 
RPIM (%) 4.6 (26.5) 
Refinement statistics  
Nonhydrogen atoms  
    Protein 10174 
    Water 
Resolution (Å) 50 – 3.4 
Rfactor (%) 24.8 
Rfree (%) 27.9 
r.m.s.d from ideality  
    Bond lengths (Å) 0.007 
    Bond angles (°) 1.53 
    Dihedrals 26.59 
    Impropers 0.963 
Ramachandran plot  
    Most favored 78.2 
    Allowed 20.0 
    Generous 1.0 
    Unfavored 0.8 
B-factors (Å2 
    Average per residue 110 

The values in parentheses are for the highest resolution bin (approximate interval 0.1 Å). RPIM is Rmerge divided by the root square of the redundancy (reference 53). Rfactor = 100⋅Σhkl | |Fo| - |Fc| | / Σhkl |Fo| for all data except for 5%, which was used for the Rfree calculation.

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