Skip to main content

Advertisement

Table 1 Data collection and refinement statistics

From: Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties

  SAD Native
Data collection   
   Resolution (Å) 30–2.3 50–2.1
   Wavelength (Å) 0.9792 0.9795
   Total reflections 1,996,840 1,197,490
   Unique reflections 29,848 38,527
   Completeness (%) 99.8 (99.8)a 99.9 (100)a
   Rsym (%)b 11.9 (32.2) 13.7 (64.3)
   Average I/σ(I) 30.4 (6.7) 17.0 (3.1)
Refinement   
   Resolution (Å) 50–2.1  
   Rcryst (%)c 22.3  
   Rfree (%)d 26.4  
   Protein atoms 4,469  
   Water molecules 138  
   RMS deviations   
Bond lengths (Å) 0.0095  
Bond angles (°) 1.50  
   Ramachandran plot (%)e   
Most favored 92.0  
Additionally allowed 7.2  
Generally allowed 0.8  
Disallowed 0  
  1. aValues in parentheses are for the highest-resolution shell (2.38–2.30 Å for SAD and 2.18–2.10 Å for native).
  2. bRsym = Σ|(I hkl ) - <I>|/Σ(I hkl ), where I hkl is the integrated intensity of a given reflection and <I> is the mean intensity of symmetry equivalents.
  3. cRcryst = Σ||Fobs| - |F calc ||/Σ|F obs |, where Fobs and F calc are the observed and calculated structure factors, respectively.
  4. dRfree is the R-factor calculated using a randomly selected 5% of reflection data withheld from the refinement.
  5. eCalculated with the program PROCHECK [36].