Table 1 Data collection and refinement statistics (molecular replacement)

From: High-resolution crystal structure of arthropod Eiger TNF suggests a mode of receptor engagement and altered surface charge within endosomes

 

S. frugiperda Eiger TNF domain

Data collection

Space group

R 3:H

Cell dimensions

  a, b, c (Å)

55.2, 55.2, 142.1

α, β, γ (°)

90, 90, 120

Resolution (Å)

47.4–1.7 (1.72–1.69)

CC (1/2)

1.0 (0.4)

R merge

0.131 (0.974)

I /σI

10.1 (1.2)

Completeness (%)

97.5 (81.2)

Redundancy

8.6 (3.5)

Refinement

Resolution (Å)

47.4–1.7 (1.72–1.69)

No. of reflections

152050 (2675)

Rwork/Rfree

15.5/18.2

No. of atoms

  Protein

1240

  Water

175

B-factors

  Protein

20.37

  Water

37.33

R.m.s. deviations

  Bond lengths (Å)

0.005

  Bond angles (°)

1.15

  1. Statistics for the highest-resolution shell are shown in parentheses