Table 1 Data collection, phasing and refinement statistics.

From: Structural insight in the toppling mechanism of an energy-coupling factor transporter

 

FolT1

AMPPNP bound ECFFolT2

apo ECFFolT2

Data collection

 Space group

C121

P1

P1

 Cell dimensions

   

a, b, c (Å)

108.91, 77.54, 89.45

90.07, 97.26, 105.45

88.82, 95.32, 107.57

α, β, γ (°)

90.0, 116.36, 90.0

84.67, 64.78, 62.59

83.45, 65.75, 61.99

 Resolution (Å)

43.0–3.01 (3.32–3.01)*

43.9–3.30 (3.40–3.30)*

49.0–3.00 (3.07–3.00)*

Rmerge

0.12 (0.38)*

0.026 (0.86)*

0.04 (0.92)*

II

5.3 (2.18)*

12 (1.10)*

10.5 (1.65)*

 Completeness (%)

82.3 (44)*

94.4 (78.8)*

92.6 (86.6)*

 Redundancy

2 (1.8)*

1.8 (1.7)*

1.8 (1.72)*

Refinement

 Resolution (Å)

3.01

3.30

3.00

 No. of reflections

10,960

33,723

41,549

Rwork/Rfree

0.235/0.286

0.252/0.294

0.232/0.279

 No. of atoms

2,456

15,554

15,398

Protein

2,392

15,430

15,398

Ligand/ion

64

124

Water

B-factors

   

Protein

36

159

98

Ligand/ion

17

158

Water

 R.m.s. deviations

   

Bond lengths (Å)

0.011

0.006

0.005

Bond angles (°)

1.429

1.404

1.263

  1. For each structure, one crystal was used for data collection.
  2. *Values in parentheses are for the highest-resolution shell.