Table 1. Summary of data collection and refinement statistics for the Keap1-DCNeh2 peptide complex.
| Data collection | |
| Source | RAXIS IV++ |
| Wavelength () | 1.5418 |
| Space group | P61 |
| Unit cell () | a = b = 103.13, c = 56.14, = 120 |
| Resolution () | 20.01.9 |
| Completeness (%)† | 98.2 (88.0) |
| Redundancy | 8.6 (3.6) |
| R merge (%)‡ | 8.6 (39.8) |
| Refinement statistics | |
| No. of complex molecules in a.u. | 1 |
| Resolution limit () | 20.01.9 |
| cutoff (F) | 0 |
| No. of reflections | 25143 |
| R work/R free (%)§ ¶ | 17.2/21.1 |
| No. of protein residues | 295 |
| No. of peptide residues | 6 |
| No. of SO4 ions | 7 |
| No. of water molecules | 307 |
| Average B-factor (2) | |
| Protein | 32.5 |
| Water | 45.5 |
| r.m.s. deviations | |
| Bond lengths () | 0.016 |
| Bond angles () | 1.55 |
†
Numbers in parentheses are values in the highest resolution shell (1.951.90).
‡
R merge = h i|I(h)i I(h)|/h i I(h)i, where I(h) is the observed intensity of reflection h, I(h) is the mean intensity of reflection h over all measurements of I(h), h is the sum over all reflections and i is the sum over i measurements of reflection h.
§
R work = ||F obs| |F calc||/|F obs|.
¶
R free was calculated with 5% of data omitted from the refinement.