Skip to main content

Table 1 Data collection and refinement statisticsa

From: Cofactor-mediated conformational control in the bifunctional kinase/RNase Ire1

Data collection and refinement Statistics Subcategory Value
Data collection Cell dimensions Space group C222
   a, b, c (Å) 91.67, 580.82, 177.99
   α, β, γ (°) 90, 90, 90
   Resolution (Å) 97-6.60 (6.8-6.60)
   I/σ(I) 16.62 (1.09)
   Rpimb (%) 4.4 (88.3)
   Number of reflections 9402 (766)
   Completeness (%) 99.9 (99.9)
Data refinement Number of atoms (in one monomer) Protein 3399
   Resolution (Å) 97-6.60
  Rigid body (with NCS) Angles (o) 0.925
   Bonds (Å) 0.006
   Rwork/Rfree 0.2863/0.3170
  Simulated annealing (with NCS) t (°K) 1,000
   Angles (°) 1.197
   Bonds (Å) 0.007
   Rwork/Rfree 0.2731/0.3451
  1. aRefinement was done using rigid body protocol. Simulated annealing was not used in final analysis, except for calculations of omit maps. Values for the highest resolution shell are shown in parentheses. bPrecision-indicating merging R-factor [42].
  2. Definitions: NCS - non-crystallographic symmetry; Rpim - precision-indicating merging factor; Rwork - crystallographic residual factor; Rfree - free crystallographic residual factor.