Table 3 Table of peptide microcrystal data collection and refinement statistics

From: Identifying amyloid-related diseases by mapping mutations in low-complexity protein domains to pathologies

 

58SGMGGIT64

58SGMGCIT64

52GGYAGAS58

Data collection

   

 Space group

P21

P21

P1

 Cell dimensions

   

 a, b, c (Å)

8.36, 51.61, 9.53

4.75, 46.17, 10.33

9.43, 10.49, 16.63

 α, β, γ (°)

90.0,109.1,90.0

90.0, 103.3, 90.0

88.9, 76.3, 74.1

 Resolution (Å)

1.1

1.7

1.1

 Rsym or Rmerge

0.182 (0.351)

0.192 (0.947)

0.059 (0.109)

 I / σI

3.3 (1.4)

13.0 (2.1)

7.43 (3.93)

 Completeness (%)

93.3 (62.7)

93.5 (71.4)

72.0 (50.7)

 Redundancy*

2.6 (2.0)

4.4 (2.6)

1.5 (1.5)

Refinement

   

 Resolution (Å)

1.1

1.7

1.1

 No. reflections

7,713

2,087

3,928

 Rwork / Rfree

0.157 / 0.169

0.291 / 0.269

0.280 / 0.306

No. atoms

   

 Protein

98

43

41

 Ligand/ion

19

4

0

 Water

N/A

N/A

N/A

B-factors

   

 Protein

9.1

30.1

7.1

 Ligand/ion

18.0

34.1

N/A

 Water

N/A

N/A

N/A

R.m.s. deviations

   

 Bond lengths (Å)

0.010

0.022

0.001

 Bond angles (°)

1.5

2.0

0.6

  1. *Single crystals were used for structure determination of SGMGGIT and GGYAGAS. Data from two crystals were merged for SGMGCIT. Values in parentheses are for highest-resolution shell.
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