Table 3. Data collection and phasing of trypsin by S-SAD, thermolysin by Zn-SAD and FAE by Se-SAD.
Statistics for the highest-resolution shell are shown in parentheses.
| Protein | Trypsin | Thermolysin | FAE |
|---|---|---|---|
| Data collection | |||
| Energy (keV) | 6 | 9.672 | 12.662 |
| Resolution range (Å) | 50.0–2.2 (2.27–2.2) | 50–1.43 (1.45–1.43) | 50–1.7 (1.73–1.71) |
| Space group | P212121 | P6122 | P41212 |
| Unit cell (Å, °) | 60.0, 64.1, 69.7 90, 90, 90 | 92.7, 92.7, 128.6 90, 90, 120 | 112.0, 112.0, 65.9 90, 90, 90 |
| Unique reflections | 13845 (1057) | 60230 (2 379) | 207445 (11053) |
| Anom. multiplicity | 11.8 (6.5) | 2.8 (2.0) | 2.4 (2.3) |
| Anom. completeness (%) | 97.2 (85.8) | 96.7 (60.6) | 96.3 (96.1) |
| Mean 〈I/σ(I)〉 | 24.9 (10.4) | 13.6 (3.7) | 11.2 (0.9) |
| Wilson B factor (Å2) | 15.1 | 11.3 | 24.2 |
| (I/σ)asymptotic † | 12.1 | 9.8 | 19.0 |
| R p.i.m. (%)‡ | 2.4 (7.4) | 4.2 (13.7) | 4.1 (84.1) |
| CC* | 0.997 (0.98) | 0.99 (0.93) | 0.997 (0.318) |
| Anom. mid-slope§ | 1.136 | 1.224 | 1.293 |
| SigAno | 1.23 (0.76) | 1.48 (1.57) | 1.44 (0.7) |
| Structure refinement | |||
| R work (%) | 17.6 (19.7) | 14.5 (19.0) | 18.3 (36.4) |
| R free (%) | 22.0 (27.5) | 16.4 (19.6) | 20.1 (37.1) |
| No. of non-H atoms | 1830 | 2948 | 2358 |
| Macromolecules | 1636 | 2561 | 2232 |
| Water | 170 | 362 | 50 |
| Ligand/ion/glycerol | 24 | ||
| R.m.s.d. (bonds, Å) | 0.008 | 0.017 | 0.02 |
| R.m.s.d. (angles, o) | 1.3 | 1.7 | 1.7 |
| Ramachandran plot (%) | |||
| Favored | 97.3 | 97.3 | 97.9 |
| Allowed | 2.7 | 2.7 | 2.1 |
| Average B factor (Å2) | |||
| Macromolecules | 10.2 | 8.7 | 20.7 |
| Ligand/ion/glycerol | 36.0 | 32.6 | |
| Solvent | 26.6 | 27.6 | 23.5 |
| Diffraction images | https://doi.org/10.15785/SBGRID/541 | https://doi.org/10.15785/SBGRID/542 | https://doi.org/10.15785/SBGRID/543 |
| PDB code | 6fid | 6fj2 | 6fj4 |