X-ray diffraction data collection and refinement statistics for Ls-AChBP–neonicotinoid complexes
See text for abbreviations of the neonicotinoid names.
| Gln55Arg Mutant Imidacloprid | Gln55Arg Mutant Clothianidin | Wild-Type Thiacloprid | Gln55Arg Mutant Thiacloprid | Wild-Type CH-IMI | Gln55Arg Mutant CH-IMI | Wild-Type DN-IMI | Gln55Arg Mutant DN-IMI | Gln55Arg Mutant Br-Clothianidin (Br ano)a | Wild-Type Thiacloprid (S ano)a | Gln55Arg Mutant Thiacloprid (S ano)a | |
|---|---|---|---|---|---|---|---|---|---|---|---|
| Data collection | |||||||||||
| Beamlineb | BL44XU | BL44XU | BL44B2 | BL44XU | BL44B2 | BL44XU | BL44B2 | BL26B2 | BL44B2 | BL44B2 | BL44B2 |
| Wavelength (Å) | 0.9 | 0.9 | 0.919 | 0.9 | 0.919 | 0.9 | 0.9 | 0.9 | 0.919 | 1.75 | 1.75 |
| Space group | P65 | P65 | P65 | P65 | P65 | P65 | P212121 | P212121 | P65 | P65 | P65 |
| Cell dimensions a, b, c (Å) | 74.6, 74.6, 350.7 | 74.1, 74.1, 351.6 | 74.5, 74.5, 351.0 | 74.5, 74.5, 350.8 | 74.7, 74.7, 351.0 | 74.8, 74.8, 351.4 | 77.0, 118.4, 243.6 | 73.1, 120.7, 139.3 | 74.8, 74.8, 351.8 | 74.6, 74.6, 351.2 | 74.6, 74.6, 350.9 |
| Resolution (Å) | 18.1–2.52 | 39.6–2.67 | 47.5–2.24 | 39.6–2.68 | 47.6–2.30 | 18.0–2.48 | 50.0–2.09 | 50.0–2.25 | 50–3.2 | 50.0–2.90 | 50.0–3.0 |
| Rsym (%)c,d | 8.7 (40.0) | 9.4 (40.2) | 9.1 (43.8) | 8.4 (40.3) | 7.7 (41.4) | 9.9 (37.5) | 7.4 (46.3) | 7.6 (44.9) | 13.8 (36.2) | 10.3 (30.8) | 8.9 (34.0) |
| I/σχ | 8.4 (1.9) | 6.9 (1.8) | 37.2 (5.20) | 7.8 (1.8) | 24.9 (2.42) | 6.4 (2.0) | 24.7 (2.30) | 38.5 (4.44) | 19.4 (8.4) | 64.7 (16.5) | 47.8 (11.5) |
| Completeness (%)c | 99.7 (100) | 99.6 (99.9) | 99.9 (100) | 98.9 (99.9) | 99.0 (91.1) | 99.5 (99.5) | 99.2 (93.7) | 99.8 (99.7) | 100 (100) | 99.8 (99.6) | 95.3 (97.4) |
| Redundancyb | 5.1 (5.1) | 3.4 (3.4) | 11.2 (10.3) | 2.6 (2.6) | 10.9 (7.9) | 5.2 (5.2) | 7.1 (6.4) | 7.3 (7.0) | 14.6 (14.8) | 22.1 (22.0) | 22.8 (23.2) |
| Refinement | |||||||||||
| Resolution (Å) | 18.1–2.54 | 39.6–2.68 | 47.5–2.24 | 39.6–2.69 | 47.6–2.30 | 18.0–2.48 | 47.8–2.09 | 20.8–2.25 | |||
| No. reflections | 35,965 | 30,443 | 52,420 | 30,084 | 48,471 | 37,741 | 131,114 | 58,862 | |||
| R/Rfree (%)e | 19.7/27.1 | 19.3/26.0 | 22.2/26.6 | 20.0/27.4 | 21.0/26.5 | 20.3/26.2 | 21.3/26.2 | 21.5/26.2 | |||
| Bond length (Å)/angles (deg)f protein (ligands) | 0.008/1.3 (0.004/0.29) | 0.007/1.3 (0.001/0.16) | 0.007/1.3 (0.004/0.25) | 0.008/1.3 (0.004/0.31) | 0.006/1.3 (0.003/0.15) | 0.008/1.6 (0.003/0.14) | 0.006/1.3 (0.003/0.16) | 0.007/1.4 (0.004/0.25) | |||
| B factor protein (ligands) | 38.9 (39.0) | 48.0 (50.1) | 38.2 (41.1) | 46.9 (48.7) | 40.7 (32.0) | 37.3 (28.6) | 38.5 (31.1) | 43.8 (29.8) | |||
| PDB codeg | 3WTH | 3WTI | 3WTJ | 3WTK | 3WTL | 3WTM | 3WTN | 3WTO |
↵a Data sets for detection of anomalous peaks at sulfur, bromine, and chlorine atoms.
↵b All data sets were collected at SPring-8.
↵c Values in parentheses refer to data in the highest resolution shells.
↵d Rsym = Σ|I-<I>|/ΣI, where I is the observed intensity and <I> is the average intensity from multiple observations of the symmetry-related reflections.
↵e R = Σ||Fo| – |Fc|| / Σ|Fo|. Rfree is an R factor of the either CNS or Refmac5 refinement evaluated for 5% of reflections that were excluded from the refinement.
↵f Root mean square deviations (rmsd) from ideal values were calculated using either CNS, CCP4, or PHENIX for the protein parts, and Mogul for the ligand parts.
↵g The atomic coordinates and structure factors have been deposited in the Protein Data Bank.