Table 2.
Data collection and structure determination of bovine PERK luminal domain complexed with the peptide substrate P16
| Native | |
|---|---|
| Data collection | |
| Space group | P21 |
| Cell dimensions | |
| a, b, c (Å) | 60.75 161.55 104.78 |
| α, β, γ (°) | 90.00 106.84 90.00 |
| Wavelength(Å) | 1.000 |
| Resolution (Å) | 43.31–2.80 (2.85 – 2.80)a |
| Rsym or Rmerge | 0.081 (0.437) |
| I/σI | 20.8 (2.1) |
| Completeness (%) | 91.5 (94.5) |
| Redundancy | 3.0 (2.9) |
| Refinement | |
| Resolution (Å) | 2.80 |
| No. reflections | 43,538 (3090) |
| Rwork/Rfree | 0.242 (0.325)/0.293 (0.313) |
| No. atoms | |
| Protein | 7268 |
| Ligand/ion | |
| Water | 173 |
| B-factors | |
| Protein | 55.05 |
| Ligand/ion | |
| Water | 58.35 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.005 |
| Bond angles (°) | 0.710 |
a Highest-resolution shell is shown in parentheses.