Table 2.
X-ray diffraction data and refinement statistics for the steric zippers that are responsible for amyloid fibril assembly by VLs
Each structure was derived from a single crystal.
| ASLTVS PDB 6DJ0 | NFVFGT PDB 6DIX | YTFGQ PDB 6DIY | |
|---|---|---|---|
| Data collection | |||
| Space group | P21 | P1 | C2 |
| Cell dimensions | |||
| a, b, c (Å) | 15.16, 11.58, 18.8 | 16.03, 11.66, 21.94 | 36.87, 4.81, 18.91 |
| α, β, γ (°) | 90, 97.32, 90 | 90.89, 103.23, 90.26 | 90, 104.95, 90 |
| Resolution (Å) | 18.6–1.3 | 20.0–1.0 | 18.3–0.9 |
| Rsym or Rmerge (%) | 19.2 (27.0)a | 6.6 (12.4) | 6.2 (21.8) |
| I/σI | 3.7 (1.7) | 12.8 (6.7) | 14.1 (3.2) |
| Completeness (%) | 80.5 (62.5) | 81.7 (62.0) | 90.7 (49.8) |
| Redundancy | 2.5 (1.5) | 3.4 (3.2) | 5.1 (3.0) |
| Refinement | |||
| Resolution (Å) | 18.64–1.3 | 21.3–1.0 | 18.3–0.9 |
| No. of reflections | 1215 | 6154 | 2228 |
| Rwork/Rfree | 18.2/21.8 | 10.4/12.5 | 9.7/12.0 |
| No. of atoms | |||
| Peptide | 93 | 388 | 82 |
| Water | 6 | 18 | 1 |
| B-Factors | |||
| Peptide | 6.4 | 7.1 | 5.2 |
| Water | 12.8 | 21.2 | 23.2 |
| Root mean square deviations | |||
| Bond lengths (Å) | 0.019 | 0.015 | 0.013 |
| Bond angles (°) | 2.1 | 2.0 | 1.4 |
| Crystallization conditions | |||
| 0.1 m MMT (dl-malic acid/MES/Tris base; 1:2:2) (pH 5), 25% w/v PEG 1500 | 0.1 m imidazole HCl (pH 8.0), 20% w/v PEG 3000, 0.2 m zinc acetate | 2.8 m sodium acetate, 0.1 m Bistris propane (pH 7.0) | |
a The highest resolution shell is shown in parentheses.