Table 1 Data collection and refinement statistics

From: Structural insight into the Ragulator complex which anchors mTORC1 to the lysosomal membrane

 

Lamtor4-Lamtor5

The Ragulator complex

Data collection

 Beamline

BL19U1

BL19U1

 Space group

P32

P6122

 Cell dimensions

a, b, c (Å)

76.67, 76.67, 52.94

126.68, 126.68, 614.51

α, β, γ (deg.)

90, 90, 120

90, 90, 120

 Resolution (Å)

50–2.03 (2.10–2.03)

50–3.10 (3.21–3.10)

 Rmerge (%)

9.0 (>100.0)

20.1 (>100.0)

 I/σI

20.5 (1.75)

28.5 (2.25)

 CC1/2

0.548

0.797

 Completeness (%)

100.0 (100.0)

100.0 (100.0)

 Redundancy

10.3 (9.2)

34.6 (20.3)

 Wilson-plot B factor

24.5

52.1

 Molecules/asymmetric unit

2 complexes

3 complexes

Refinement

 Resolution (Å)

50–2.03

50–3.10

 Number of reflections

19 847

47 579

 Rwork/Rfree

21.64%/26.24%

22.27%/28.33%

 No. of atoms

Protein

2 542

11 608

Solvent

68

0

 B factors (Å2)

Overall

13.53

58.51

Protein

13.13

58.51

Solvent

28.53

N/A

 RMSD bond length (Å)

0.0070

0.0056

 RMSD bond angles (deg.)

1.4407

1.2122

 Ramachandran plot

Favored (%)

93.4

94.8

Allowed (%)

6.3

4.9

Disallowed (%)

0.3

0.3

  1. Abbreviations: ASU, asymmetric unit; N/A, not applicable; RMSD, root-mean-square deviations from ideal geometry.
  2. Rmerge=ΣhΣi |Ih,i−Ih|/ΣhΣi Ih,i for the intensity (I) of observation i of reflection h. R factor=Σ||Fobs|−|Fcalc||/Σ|Fobs|, where Fobs and Fcalc are the observed and calculated structure factors, respectively. Rfree=R factor calculated using 5% of the reflection data chosen randomly and omitted from the start of refinement. Data for the highest resolution shell are shown within parentheses.
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