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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]
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BMC Structural Biology

ISSN: 1472-6807

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