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Table 1 Crystallographic data

From: Active site plasticity revealed from the structure of the enterobacterial N-ribohydrolase RihA bound to a competitive inhibitor

Data collection   
Resolution range (Å) 37.5-2.1 2.21-2.1
Number of observed reflections 232,754 31,773
Number of unique reflections 68,457 9,929
Completeness (%) 97.2 95.4
Multiplicity 3.4 3.2
Mean I/σ(I) 8.1 3.0
Rsym 0.122 0.388
Refinement   
Resolution range (Å) 37.50-2.1 2.15-2.1
Number of reflections (F > 0) 65,238 4,760
Rcrys 0.203 0.254
Rfree 0.241 0.304
rmsd bonds (Å) 0.020  
rmsd angles (°) 1.689  
Mean B factor (Å2) 30.3  
Model quality   
Residues in favored regions of Ramachandran plot (%) 97.8  
Residues outliers in Ramachandran plot (%) 0.5  
Unusual rotamers (%) 0.9  
  1. Data collection and refinement statistics for the RihA-DAPIR complex.
  2. Rsym = ∑ hkl i||Ii(hkl)|-|<I(hkl)||>|/∑hkli|Ii(hkl)|, where Ii(hkl) is the ith measurement of reflection hkl, and <I(hkl)> is the average value from the individual measurements
  3. Rcrys = ∑ hkl ||Fo(hkl)|-|Fc(hkl)||/∑ hkl |Fo(hkl)|, where Fo(hkl) and Fc(hkl) are the measured and calculated structure factor of reflection hkl, respectively
  4. Rfree, same as Rcrys, but calculated on a subset of randomly-selected reflection excluded from all stages refinement (3,455 total, 265 in the highest resolution shell).