Table II. X-ray data collection and refinement statistics
A11B12A
Data collection
 Space groupP212121C2
 Unit cell dimension (Å)a = 89.2, b = 102.6, c = 118.5, α = 90.0, β = 90.0, γ = 90.0a = 128.0, b = 43.6, c = 98.4, α = 90.0, β = 125.9, γ = 90.0
 Resolution range (Å)50.0−2.60 (2.65−2.60)a40.0−2.43 (2.47−2.43)a
 Unique reflections32,187 (1,262)16,078 (603)
 Average redundancy9.9 (4.0)6.6 (3.5)
 Rmerge (%)b9.5 (48.7)12.5 (38.5)
 I/σ (I)23.0 (2.1)13.6 (2.1)
 Completeness (%)94.7 (68.4)95.0 (74.8)
Refinement statistics
 Refinement resolution (Å)34.0−2.60 (2.67−2.60)a39.7−2.43 (2.59−2.43)a
 Rcryst (%)c20.5 (26.4)20.5 (23.9)
 Rfree (%)25.8 (39.1)25.0 (31.5)
 Protein atoms6,9933,520
 Water molecules14248
 rmsd from ideal values
 Bond length (Å)0.010.01
 Bond angle (°)1.291.26
 Mean B-factor (Å2)71.662.3
 Wilson plot B-factor (Å2)69.559.4
 Ramachandran statistics
 Most favored region, %93.294.5
 Additionally allowed, %6.85.5
  • a Values for the highest resolution shell in data collection and refinement are listed in the parentheses.

  • b Rmerge = ∑hi|Ii(hkl) − < I (hkl)>|/∑hiIi(hkl).

  • c Rcryst = ∑||Fo| − |Fc||/∑|Fo| calculated from working data set. Rfree is calculated from 6.0% of data randomly chosen not to be included in refinement.