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 (Ã…)

91.67, 580.82, 177.99

  

α, β, γ (°)

90, 90, 90

  

Resolution (Ã…)

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 (Ã…)

97-6.60

 

Rigid body (with NCS)

Angles (o)

0.925

  

Bonds (Ã…)

0.006

  

Rwork/Rfree

0.2863/0.3170

 

Simulated annealing (with NCS)

t (°K)

1,000

  

Angles (°)

1.197

  

Bonds (Ã…)

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.