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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 (Ã…)

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].