Table 1 Data collection and refinement statistics

From: Structure of amyloid-β (20-34) with Alzheimer’s-associated isomerization at Asp23 reveals a distinct protofilament interface

 

Aβ20–34

Aβ20–34, isoAsp23

Data collection

Space group

P21

P21

Cell dimensions

  a, b, c (Å)

33.17, 4.78, 30.33

29.20, 4.87, 32.44

 α, β, γ (°)

90.00, 111.10, 90.00

90.00, 101.90, 90.00

Resolution (Å)

1.10 (1.13–1.10)a

1.05 (1.20–1.05)b,c

Rsym or Rmerge (%)

18.9

19.7

I/σI

5.41 (3.28)

3.76 (1.38)

Completeness (%)

85.2

82.7 (53.0)

Redundancy

6.67 (6.14)

4.19 (3.10)

Refinement

Resolution (Å)

7.74–1.10 (1.26–1.10)

5.96–1.05 (1.20–1.05)

No. of reflections

3544 (1141)

3943 (1167)

Rwork/Rfree (%)

19.4/21.3 (21.3/26.9)

19.7/24.6 (27.0/32.4)

No. of atoms

  Protein

210

204

  Ligand/ion

0

0

  Water

7

4

B-factors

  Protein

6.50

8.29

  Ligand/ion

—

—

  Water

20.78

27.70

R.m.s. deviations

  Bond lengths (Å)

0.56

1.04

  Bond angles (°)

0.68

0.90

  1. aTen crystals were used in determining the Aβ20–34 structure
  2. bFive crystals were used in determining the Aβ20–34, isoAsp23 structure
  3. cValues in parentheses are for the highest-resolution shell
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