Table 2 X-ray crystallography data collection and refinement statistics

Space group

P3₁21

P3₁21

P 4₂2₁2

P2₁2₁2

P 4₁22

Cell dimensions

a, b, c (Å)

78.3, 78.3, 127.1

73.2, 73.2, 131.7

156.4, 154.4, 116.3

149.7, 150.4, 119.5

154.6, 154.6, 229.3

α, β, γ (°)

90, 90, 120

90, 90, 120

90, 90, 90

90, 90, 90

90, 90, 90

Resolution (Å)^a

46–1.80 (1.85–1.80)

57–1.85 (1.90–1.85)

60–3.31 (3.37–3.31)

105–2.72 (2.96–2.72)

128–3.29 (3.35–3.29)

R_merge

0.109 (1.7)

0.086 (2.05)

0.091 (3.9)

0.168 (1.6)

0.82 (–)

R_pim

0.036 (0.54)

0.028 (0.46)

0.018 (0.77)

0.047 (0.46)

0.094 (4.1)

I/σ (I)

20.6 (1.9)

18.2 (1.7)

21.9 (0.5)

11.2 (1.6)

4.9 (0.2)

CC_1/2

1.0 (0.7)

1.0 (0.7)

1.0 (0.3)

1.0 (0.5)

1.0 (0.4)

Completeness (%)

99.7 (99.7)

99.8 (99.5)

100 (100)

65 (14)

100 (93)

Completeness (%) (ellipsoidal)^b

95.6 (82.1)

Redundancy

19.7 (20.1)

19.7 (20.9)

25.6 (26.5)

13.7 (12.4)

78.4 (77.9)

Resolution (Å)

46.3–1.80 (1.85–1.80)

57.2–1.85 (1.90–1.85)

128–3.31 (3.4–3.31)

78–2.71 (2.96–2.71)

128–3.29 (3.4–3.29)

No. reflections

40,120 (3,066)

35,506 (2,585)

20,977 (1,538)

47,412 (2,371)

39,015 (1,538)

R_work/R_free

16.6/19.3 (30.5/29.2)

18.5/21.7 (30.0/33.3)

26.3/30.5 (40.5/41.6)

19.8/24.1 (28.8/29.9)

23.7/26.8 (41.5/37.9)

No. atoms

Protein

2,571

2,591

5,906

11,731

11,718

Ions/buffer

64

19

–

–

–

Water

241

103

–

–

–

Residual B factors

Protein

38

28

118

65

157

Ligand/ion

55

71

–

–

–

Water

45

53

–

–

–

R.m.s. deviations

Bond lengths (Å)

0.010

0.012

0.008

0.004

0.004

Bond angles (°)

1.4

1.68

1.63

0.74

1.39