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. Author manuscript; available in PMC: 2011 Apr 16.
Published in final edited form as: J Mol Biol. 2010 Feb 22;397(5):1307–1315. doi: 10.1016/j.jmb.2010.02.028

Table 1.

Data collection, phasing and refinement statistics for P58(IPK) TPR fragment structure

Se-Met
Data collection
Space group P21
Cell dimensions
a, b, c (Å) 84.041, 93.186, 84.412
 α, β, γ (°) 90, 119.500, 90
Peak
Wavelength(Å) 0.9789
Resolution (Å) 2.5
Rsym or Rmerge 0.060 (0.184)
I/sigmaI 20.7 (4.57)
Completeness (%) 89.4 (89.2)
Redundancy 5.6 (5.3)
Refinement
Resolution (Å) 2.5
No. reflections 33419
Rwork/Rfree 23.8/29.6
No. atoms
 Protein 5762
 Water 106
B-factors
 Protein 41.6
 Water 42.9
R.m.s deviations
 Bond lengths (Å) 0.009
 Bond angles (°) 1.118
*

Highest-resolution shell is shown in parentheses.

Rsym=[ΣhklΣi|Ii−<I>|]/ΣhklΣi <I>