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Table 1 X-ray Diffraction Data and Refinement Statistics

From: Evidence for alternative quaternary structure in a bacterial Type III secretion system chaperone

Diffraction Data    
Crystal   IpgC10-155 IpgC21-155
Beamline   APS 22 - BM APS 22-ID
Wavelength (Å)   1.000 1.000
Space Group   P 21 P 31 or P 32
Cell Constants   a = 140.50 a = 86.11
   b = 71.47 b = 86.11
   c = 171.01 c = 476.27
   ß = 93.86°  
Resolution (Å)   50-3.30 50-3.40
Completeness (%)   88.5 (49.6) 89.3 (79.1)
Total Reflections   151,044 89,308
Unique Reflections 45,608 48,191
Redundancy   3.4 1.9
Rmerge(%)a   14.9 (50.7) 10.0 (33.2)
I/σ   7.3 (1.4) 7.0 (1.8)
Refinement    
Rwork/Rfreeb   25.9/29.6  
B factor (Å2)   98.23  
RMSD    
  Bond Length (Å) 0.011  
  Bond Angle (°) 1.29  
  Dihedral Angle (°) 19.67  
Ramachandran    
  Favored (%) 91.50  
  Allowed (%) 5.80  
Protein atoms   20,070  
  1. aRmerge = Σ h Σ i |I i (h)-<I(h)>|/Σ h Σ i I i (h), where I i (h) is the i th measurement of reflection h and <I(h)> is a weighted mean of all measurements of h.
  2. bR = Σ h |Fobs(h)-Fcalc(h)|/Σ h |Fobs|. Rcryst and Rfree were calculated from the working and test reflection sets, respectively. The test set constituted 5% of the total reflections not used in refinement.