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. 2008 May 22;27(12):1767–1778. doi: 10.1038/emboj.2008.104

Table 1.

Selected crystal and refinement data for ThKaiBa

Data collection
 Space group P21212
 Cell dimensions a, b, c (Å) 100.13, 191.22, 34.34
 Wavelength (Å) 1.08
 Resolution (last shell; Å) 50–2.78 (2.89–2.78)
 Unique reflections 16 993 (1797)
 Completeness (%) 98.5 (97.3)
R-merge 0.047 (0.239)
I/σ(I) 30.3 (5.3)
   
Refinement
 Working set reflections (F⩾2σF) 13 727
 Test set reflections (F⩾2σF) 1520
 Protein atoms 4808
 Solvent atoms 63
R-work/R-free (%) 0.233/0.284
 Average B-factors (Å2)  
  Protein (all residues) 98
  Protein (core residues 8–94) 93
  Solvent 99
 r.m.s. deviations  
  Bond lengths (Å) 0.008
  Bond angles (deg) 1.5
 Ramachandran analysis (%)  
  Most favoured 71.4
  Allowed 25.6
  Generously allowed 3.0
aValues in parentheses refer to the last resolution shell.