Table 1.
Parameters for crystallography with statistics from data collection, refinement, and validation
| Parameter or statistic | WT | S393A |
|---|---|---|
| Data collection | ||
| Space group | P1 | P21 |
| Unit cell: a, b, c(Å) | 85.5, 94.7, 123.0 | 71.2, 68.5, 97.7 |
| α, β, γ (deg) | 90.0, 90.4, 116.8 | 90.0, 91.7, 90.0 |
| Wavelength (Å) | 0.97872 | 0.97856 |
| Resolution (Å) | 30-2.05 (2.09–2.05) | 30-1.95 (1.98–1.95) |
| Observed reflections (n) | 219,399 (10,837) | 63,885 (3419) |
| Rmerge (%) | 4.7 (35.4) | 4.5 (47.3) |
| Completeness (%) | 97.9 (97.0) | 98.0 (97.8) |
| I/σI | 15.0 (2.1) | 25.5 (3.0) |
| Phasing method | MR | MR |
| Refinement and validation | ||
| Rwork/Rfree (%) | 16.95/21.60 (24.8/27.2) | 16.60/19.48 (22.6/24.5) |
| AMP/GOL | 3 Na, EDO, 4 GOL, 38 SO4 | 6 Ca, 1 Cl |
| Solvent molecules | 1511 | 487 |
| Bond lengths (Å) | 0.011 | 0.011 |
| Bond angles (deg) | 1.35 | 1.38 |
| Ramachandran (%) | ||
| Most favored regions | 88.1 | 87.3 |
| Additionally allowed regions | 11.8 | 12.4 |
| Generously allowed regions | 0.1 | 0.3 |
| Disallowed regions | 0.0 | 0.0 |
| PDB ID | 3QFH | 3T41 |
High-resolution shell statistics are shown in parentheses. Total number of residues in the protein is 430 from residues 28–457. The 3QFH structure has 8 molecules in the asymmetric unit (chains A–H) and has 6 missing residues between the prodomain and protease domain for chain A, 5 for chain B, 9 for chains C and G, and 4 for chains D, E, F, and H. The 3T41 structure has 2 molecules in the asymmetric unit, where 7 residues are missing from chain A and 10 from chain B at the C-terminal end of the protein.