Table 1 

Crystallographic statistics  
Cap32/34  
Data Collection  
Space Group  P4_{1} 
Cell Dimensions  
a, b, c (Å)  124.5, 124.5, 77.5 
α, β, γ (º)  90, 90, 90 
Resolution Range (Å)  502.2 (2.32.2) 
Number of Reflections  367874 
Number of Unique Reflections  60185 
Completeness (%)  99.8 (99.6) 
Multiplicity  
R_{merge}^{†}  14.9 (83.5) 
<I/σI>  14.2 (3.8) 
Refinement  
R_{work}^{‡}  0.226 
R_{free}^{§}  0.265 
R.m.s. deviations  
Bond lengths (Å)  0.008 
Bond angles (°)  1.36 
Ramachandran Analysis  
Residues in most favoured regions (%)  95.9 
Residues in allowed regions (%)  4.1 
Outliers (%)  0 
Model statistics  
Protein residues:  
No. in subunit A & B  514 
Bfactor A & B (Å^{2})  15.4 
Additional groups:  
Water (No. / Bfactor)  328 / 37.9 
Values in parentheses refer to the highest resolution shell.
^{†}R_{merge} = Σ_{hkl}Σ_{i}I_{i}(hkl)  < I(hkl) > / Σ_{hkl}Σ_{i}I_{i}(hkl); where I_{i}(hkl) is the intensity of the ith measurement of reflection hkl and < I(hkl) > is the mean value of I_{i}(hkl) for all i measurements.
^{‡}R_{work} = Σ_{hkl}F_{o}F_{c}/ΣF_{o},where F_{o} is the observed structure factor and F_{c} is the calculated structure factor.
^{§}R_{free} is the same as R_{cryst} except calculated with a subset, 5%, of data that are excluded from refinement calculations.
Eckert et al.
Eckert et al. BMC Structural Biology 2012 12:12 doi:10.1186/147268071212