Table 1.
Data collection and refinement statistics
| 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 |
aTen crystals were used in determining the Aβ20–34 structure
bFive crystals were used in determining the Aβ20–34, isoAsp23 structure
cValues in parentheses are for the highest-resolution shell