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Table 1 Crystallographic and Refinement Statistics

From: Interactions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymes

  CHIP U-box: UbcH5a complex
Data Collection  
Space group P212121
Unit cell  
   a, b, c (Å) 79.0, 93.4, 144.0
   α,β,γ (°) 90, 90, 90
No. molecules/asymmetric unit 2 CHIP, 2 UbcH5a
Resolution (Å) 55.00-2.90 (3.00-2.90)a
Unique reflections 24283
Completeness (%) 99.9 (100)
Redundancy 3.40 (3.42)
I/σ 8.5 (1.6)
Rmerge(%)b 8.0 (46.6)
Refinement  
Resolution (Å) 53.2-2.90 (3.08-2.90)
Rwork(%)c 24.0
Rfree(%)d 27.2
Protein atoms 3518
Waters 4
Other atoms 3
Average B factor (Å2) 65.0
r.m.s.d. – bond lengths (Å) 0.007
r.m.s.d. – bond angles (°) 1.4
r.m.s.d. – dihedrals (°) 23.4
r.m.s.d. – improper angles (°) 1.1
Ramachandran plot (%)  
   Most favored and allowed 97.6
   Generously Allowed 2.4
   Disallowed 0.0
PDB ID code 2 OXQ
  1. aStatistics for the highest resolution shell are shown in parentheses.
  2. bRmerge = Σ|Ii-<Ii>|/Σ|Ii|
  3. cRwork = Σh||Fobs(h)|-k|Fcalc(h)||/ΣhFobs(h)
  4. dRfree is the R factor calculated for 5% of reflections, excluded from refinement