TABLE 1.
X-ray data collection and refinement statistics.
| Data collection | PaHigA–DNA(28 bp) | PaHigA–DNA(18 bp) |
| Beamline | SSRF 18U1 | SSRF 18U1 |
| Wavelength (Å) | 0.9788 | 0.9788 |
| Space group | P212121 | P21 |
| Unit-cell parameters | a = 77.8 Å, b = 90.7 Å, c = 91.7 Å, α = β = γ = 90° | a = 57.3 Å, b = 95.6 Å, c = 128.9 Å, α = γ = 90°, β = 96.3 |
| Resolution (Å) | 3.14 (3.23–3.14)a | 2.50 (2.54–2.50)a |
| Number of unique reflections | 11506 (807) | 47471 (2352) |
| Completeness (%) | 98.3 (94.3) | 99.3 (99.2) |
| Redundancy | 6.6 (3.8) | 6.2 (5.6) |
| Mean I/o’ (I) | 11.20 (1.77) | 20.08 (1.64) |
| Molecules in asymmetric unit | 4 | 8 |
| Rmerge (%) | 10.9 (68.5) | 10.5 (86.5) |
| Rmeas (%) | 11.0 (75.4) | 11.4 (93.5) |
| CC1/2 | 99.9 (97.8) | 100.3 (89.3) |
| Structure refinement | ||
| Reflections used in refinement | 11436 | 47323 |
| Resolution range (Å) | 45.35–3.14 | 47.20–2.50 |
| Rwork/Rfree (%) | 21.5/28.0 | 21.8/26.2 |
| Protein atoms | 2925 | 5830 |
| Protein residues | 369 | 733 |
| Waters | 0 | 62 |
| Average B factor (Å2) | ||
| Protein | 75.56 | 65.27 |
| DNA | 79.85 | 55.62 |
| Ramachandran plot (%) | ||
| Most favored | 94.2 | 94.7 |
| Allowed | 4.7 | 3.8 |
| Disallowed | 1.1 | 1.3 |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.013 | 0.010 |
| Bond angles (°) | 1.494 | 1.179 |
aThe values in parenthesis means those for the highest resolution shell.