Table I.
Data collection and refinement statistics (molecular replacement)
| apo-SaBPL | Biotin-SaBPL | Btyl-SaBPL | |
|---|---|---|---|
| Data collectiona | |||
| Wavelength (Å) | 0.95364 | 0.99810 | 1.5418 (Cu Kα) |
| Space group | P21 | P42212 | P42212 |
| Cell dimensions | |||
| a, b, c (Å) | 50.1, 51.4, 67.6 | 94.2, 94.2, 130.9 | 93.6, 93.6, 130.7 |
| α, β, γ (°) | 90, 108, 90 | 90, 90, 90 | 90, 90, 90 |
| Resolution (Å) | 35.0–2.1 (2.16–2.1) | 40–3.2 (3.45–3.2) | 20.0–2.6 (2.67–2.6) |
| Rsym or Rmerge | 11.3 (43.3) | 5.2 (44.1) | 5.7 (36.2) |
| I/σI | 8.8 (2.8) | 11.1 (2.0) | 12.7 (2.1) |
| Completeness (%) | 96.1 (96.3) | 98.7 (92.6) | 98.3 (94.7) |
| Redundancy | 3.8 (3.9) | 4.6 (4.3) | 4.1 (3.7) |
| Refinement | |||
| Resolution (Å) | 35.0–2.1 | 30–3.2 | 20.0–2.6 |
| No. reflections | 17,599 | 9929 | 18,509 |
| Rwork/Rfree | 19.6/24.9 | 19.2/23.9 | 19.9/25.7 |
| No. atoms | |||
| Protein | 2484 | 2602 | 2602 |
| Ligand/ion | 0 | 16 | 38 |
| Water | 212 | 0 | 305 |
| B-factors | |||
| Protein | 32.1 | 57.6 | 50.8 |
| Ligand/ion | – | 58.2 | 55.2 |
| Water | 36.8 | – | 65.2 |
| R.M.S. deviations | |||
| Bond lengths (Å) | 0.019 | 0.015 | 0.022 |
| Bond angles (°) | 1.9 | 1.9 | 1.9 |
| % in most favored regions of a Ramachandran plot | 94.0 | 95.0 | 97.1 |
a
Diffraction data were collected from one crystal for each structure.