Table 1

Data collection and refinement statisticsa

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


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].

Definitions: NCS - non-crystallographic symmetry; Rpim - precision-indicating merging factor; Rwork - crystallographic residual factor; Rfree - free crystallographic residual factor.

Korennykh et al. BMC Biology 2011 9:48   doi:10.1186/1741-7007-9-48

Open Data