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Table 1 Data collection and refinement statistics

From: The backbone structure of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein is essentially identical to its mesophilic E. coli homolog

  tteRBP
Data Collection  
   Detector Type Mar225
   Wavelength (Å) 1.0
   Resolution (Å) 15.0–1.9
   Measured reflections 123829
   Unique reflections 16732
   Mean I/σ(I)a 11.6 (4.1)
   Completeness (%)a 96.0 (95.1)
   Rsym (%)a,b 8.0 (32.4)
   Redundancya 3.3 (3.1)
Refinement  
   Resolution (Å) 15.0–1.9
   Num. of Reflections (working set/test set) 35702/1890
   Rcrystc 19.9 (26.0)
   Rfreed 23.4 (30.6)
   Number of atoms  
Protein 4265
Water 346
Ligand 20
r.m.s.d.  
   Bond lengths (Å) 0.011
   Bond angles (°) 1.221
Average B-factor (Å2)  
   Main Chain 17.8
   Side Chain 22.7
   Solvent 28.7
   Ligand 10.1
Protein Geometry  
   Ramachandran outliers (%) 0.55
   Ramachandran favored (%) 98.7
   Rotamer outliers (%) 0.47
  1. aNumber in parentheses represent values in the highest resolution shell.
  2. bRsym = ∑|(I-<I>)|/(∑I), where <I> is the average intensity of multiple measurements.
  3. cRcryst = ∑|Fobs-Fcalc|/(∑|Fobs|)
  4. dRfree is the R-factor based on 5% of the data excluded from refinement.