TABLE 1.
Summary of data collection and refinement statistics
| Statistic | Value for the Keap1-DC-Neh2 peptide complexa |
|---|---|
| Data collection statistics | |
| Source | RAXIS IV++ |
| Wavelength (Å) | 1.5418 |
| Space group | P61 |
| Unit cell dimensions (Å) | a = b = 103.13, c = 56.14, γ = 120° |
| Resolution (Å) | 20.0-1.9 |
| Completeness (%) | 98.2 (88.0) |
| Redundancy | 8.6 (3.6) |
| Rmerge (%)b | 8.6 (39.8) |
| Refinement statistics | |
| No. of complex molecules | |
| (asymmetric unit) | 1 |
| Resolution limit (Å) | 20.0-1.9 |
| Sigma cutoff | 0 |
| No. of reflections | 25,143 |
| R factor/Rfree (%)c | 17.2/21.1 |
| No. of protein residues | 295 |
| No. of peptide residues | 6 |
| No. of SO4 ions | 7 |
| No. of water molecules | 307 |
| rms deviationsd | |
| Bond lengths (Å) | 0.016 |
| Bond angles (°) | 1.55 |
a
Numbers in parentheses are the values for the highest resolution shell.
b
Rmerge = Σ|Iobs − <I>|/Σ <I> summed over all observations and reflections, where Iobs is observed intensity and <I> is the mean intensity.
c
The crystallographic R factor (Rcryst) = Σ|Fobs − Fcalc|/ΣFobs, where Fobs is observed structure factors and Fcalc is calculated structure factors. Rfree was calculated with 5% of data omitted from refinement.
d
rms, root mean square.