Table 1.
Crystallographic data for bovine F1-ATPase complexed with various polyphenol inhibitors
| Resveratrol–F1 | Quercetin–F1 | Piceatannol–F1 | |
|---|---|---|---|
| Space group | P21 | P21 | P21 |
| Unit cell dimensions, Å (a, b, c) | 106.8, 277.4, 137.8 | 106.4, 282.0, 138.1 | 107.0, 281.2, 138.8 |
| Unit cell angles, ° (α, β, γ) | 90.0, 90.2, 90.0 | 90.0, 90.4, 90.0 | 90.0, 89.6, 90.0 |
| Resolution, Å | 2.30 | 2.40 | 2.70 |
| No. of unique reflections | 299,020 (40,061) | 297,401 (40,583) | 201,334 (30,153) |
| Rmerge,* % | 6.4 (23.6) | 8.2 (40.3) | 8.7 (34.9) |
| Completeness,† % | 84.7 (77.5) | 94.3 (88.1) | 90.3 (92.5) |
| Multiplicity | 1.4 (1.4) | 2.1 (2.0) | 1.4 (1.3) |
| 〈I/σ(I)〉 | 7.8 (2.1) | 7.2 (2.3) | 7.3 (1.9) |
| Wilson B factor, Å2 | 38.6 | 40.5 | 54.2 |
| Inhibitor atoms‡ | 34 | 44 | 36 |
| Water molecules | 3,847 | 2,202 | 1,113 |
| Glycerol molecules | 12 | 12 | 12 |
| R factor,§ % | 16.0 | 18.8 | 20.2 |
| Rfree,¶ % | 21.7 | 23.8 | 26.9 |
| rms deviation bonds, Å | 0.010 | 0.009 | 0.010 |
| rms deviation angles, ° | 1.2 | 1.2 | 1.3 |
Values for the highest-resolution bins (2.42–2.30, 2.53–2.40, and 2.85–2.70 Å, respectively, for the resveratrol–F1, quercetin–F1, and piceatannol–F1 complexes) are given in parentheses.
*Rmerge = Σhkl Σi|〈I(hkl)〉 − Ii(hkl)| / Σhkl Σi Ii(hkl), where 〈I(hkl)〉 is the mean weighted intensity for multiple recorded reflections i after rejection of outliers. Measurements with intensities differing >3.5 σ (I) from the weighted mean were rejected.
†The overall completeness for the resveratrol–F1 data and piceatannol–F1 data is slightly low because only 60° of data were collected.
‡Hydrogen atoms were excluded.
§The R factor is defined as Σhkl|Fo(hkl) − Fc(hkl)|/Σhkl|Fo(hkl)|, where Fo and Fc are the observed and calculated structure factor amplitudes, respectively, and was determined by using 95% of the data.
¶The free R factor is the R factor calculated for the residual 5% of the data set not included in the refinement.