Table 1.
Data Collection and Refinement Statistics for Representative XcPrxQ Structures
| Data Collection | PDB code: 5iiz | PDB code: 5imc | PDB code: 5imf | PDB code: 5iny | PDB code: 5io2 |
|---|---|---|---|---|---|
| Structure | FF0 | FF3 | FF5 | FF8 | C48S |
| Space group | P21 | P21 | P21 | P21 | P21 |
| Unit cell a, b, c (Å), γ (°) | 35.4, 52.4, 40.0, 103.3 | 35.5, 51.2, 40.0,104.0 | 35.6, 51.5, 40.0, 104.1 | 35.6, 51.3, 40.0, 104.0 | 35.6, 51.3, 39.7, 103.8 |
| Resolution (Å) | 25.5–1.05 (1.11-)a | 10.6–1.05 (1.11-) | 23.2–1.04 (1.10-) | 11.5–1.04 (1.10-) | 30.8–1.20 (1.26-) |
| Completeness (%) | 98.0 (96.7) | 87.6 (50.0) | 90.5 (51.0) | 91.0 (51.3) | 86.4 (47.6) |
| Unique reflections | 63472 (9105) | 56804 (4673) | 60776 (4940) | 60675 (4932) | 37466 (2964) |
| Multiplicity | 7.0 (6.9) | 6.6 (4.5) | 6.3 (3.8) | 6.4 (3.8) | 3.6 (3.0) |
| Rmeas (%) | 11 (147) | 8 (95) | 10 (135) | 8 (125) | 10 (75) |
| CC1/2 | 1.0 (0.70) | 1.0 (0.72) | 1.0 (0.45) | 1.0 (0.51) | 1.0 (0.71) |
| <I/σ> | 11.8 (2.3) | 15.8 (2.0) | 11.3 (0.9) | 14.3 (1.3) | 8.4 (1.6) |
| <I/σ> ~2.0 (Å)b | - | 1.05 | 1.07 | 1.06 | 1.25 |
| Refinement | |||||
| Resolution range (Å) | 25.5–1.05 | 10.6–1.05 | 23.2–1.04 | 29.6–1.04 | 30.8–1.20 |
| R-factor (%) | 13.5 | 12.5 | 13.8 | 12.3 | 13.7 |
| R-free (%) | 15.3 | 14.4 | 16.0 | 14.5 | 16.7 |
| Protein residues | 159 | 158 | 159 | 159 | 159 |
| Water molecules | 261 | 308 | 316 | 311 | 325 |
| RMSD lengths (Å) | 0.007 | 0.015 | 0.013 | 0.011 | 0.012 |
| RMSD angles (°) | 1.0 | 2.0 | 1.8 | 1.7 | 1.3 |
| Ramachandran plotc | |||||
| φ, ψ-Preferred (%) | 100.0 | 100 | 100.0 | 99.4 | 100 |
| φ, ψ-Allowed (%) | 0.0 | 0.0 | 0.0 | 0.6 | 0.0 |
| φ, ψ-Outliers (%) | 0.0 | 0.0 | 0.0 | 0.0 | 0.0 |
| B factorsd | |||||
| <Main chain> (Å2) | 11 | 8 | 8 | 9 | 9 |
| <Waters> (Å2) | 33 | 23 | 24 | 25 | 25 |
| Rxn progression (%) | pH=7.0 | pH=4.5 | pH=4.5 | pH=4.5 | pH=5.5 |
| S− | 100 | 50 | 55 | ||
| SO− | 50 | 15 | |||
| SO−inv | 10 | ||||
| SO2− | 20 | 100 | |||
a
Values in parenthesis are for the highest resolution shell and preceding values are for all data;
b
For reference to traditional resolution cutoffs, the point where <I/σ> falls to ~2.0 is provided;
c
Preferred, allowed, and outlier angles as assigned by Molprobity(Davis et al., 2004);
d
Outliers were generally in areas of weak density, such as the C-terminal region. Please also see Table S1 for crystallographic statistics for additional structures.