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Table 1 Data collection and refinement statistics of DJNK structure

From: The crystal structure of JNK from Drosophila melanogaster reveals an evolutionarily conserved topology with that of mammalian JNK proteins

Data collection  
 Space group P212121
 Unit-cell parameters (Å) a = 52.49, b = 55.33, c = 126.72
 High resolution limit (Å) 1.58
 Total reflections 219226
 Unique reflections 51133
 Average mosaicity (°) 0.0
 Completeness (%) 99.4 (97.6)a
 Redundancy 4.3(4.2)a
 b R merge (%) 6.2 (79.4)a
 I/σ(I) 11.8 (1.8)a
Refinement statistics  
 Resolution range (Å) 28.28-1.79
 Highest resolution shell (Å) 1.84-1.79
 c R-factor (%) 18.9
 d R free-factor (%) 22.4
 Averaged B-factor (Å2) 26.0
 Number of non-hydrogen atoms  
  Protein 2810
  Water 143
  ADPNP 1
  Mg2+ ions 2
 RMSD from ideal geometry  
  Bond length (Å) 1.07
  Bond angle (°) 1.06
 eRamachandran plot (%)  
  Favored regions 97.0
  Additional allowed regions 3.0
  Outliers 0
  1. aNumber in parentheses refer to the outer resolution shell
  2. b R merge =  ∑ hkl i |I hkl,i – 〈I hkl 〉|/ ∑ hkl i I hkl,i , where 〈I hkl 〉 is the mean intensity of symmetry-equivalent reflection
  3. c R-factor = ∑ |F obs-F cal|/∑F obs, where F obs and F cal are observed and calculated structure factor amplitudes, respectively
  4. d R free-factor value was calculated as R-factor but using a subset (10 %) of reflections that were not used for refinement
  5. eRamachandran plot was calculated using MolProbity [11]