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Table 2 Data collection and refinement statistics.

From: Ligand-induced conformational changes in a thermophilic ribose-binding protein

  tmRBP-apo tmRBP-ribose
Data Collection   
   Wavelength (Å) 0.997 0.979
   Resolution (Å) 1.40 2.15
   Unique reflections 115460 25783
   Mean I/σ(I)a 34.2 (1.7) 25.7 (3.6)
   Completeness (%)a 99.0 (88.8) 80.9 (21.0)
   Rsym (%)a 5.0 (51.5) 5.6 (28.4)
   Redundancya 5.8 (3.4) 5.8 (1.6)
Refinement   
   Resolution (Å) 50.0–1.40 50.0–2.15
   Num. of Reflections (working set/test set) 115460/5767 23715/1354
   Rcryst (%) 18.0 (28.0) 19.3 (25.4)
   Rfree b (%) 20.3 (32.9) 22.3 (29.2)
   Number of atoms   
Protein 4326 2286
Water 627 142
Ligand 0 10
r.m.s.d.   
   Bond lengths (Å) 0.009 0.012
   Bond angles (°) 1.2 1.2
Average B-factor (Å 2 )   
   Main Chain 15.3 34.5
   Side Chain 17.3 35.8
   Solvent 29 37.7
   Ligand   24.8
Protein Geometry   
   Ramachandran outliers (%) 0.4 0.3
   Ramachandran favored (%) 98.7 97.6
   Rotamer outliers (%) 2.2 3.0
  1. aNumber in parentheses represent values in the highest resolution shell.
  2. bRfree is the R-factor based on 5% of the data excluded from refinement.