Table 1.
The data collection and refinement statistics for the free D70N and D70N–DNA complex structures
| RusA D70N | RusA-D70N–DNA complex | |
|---|---|---|
| Data collection | ||
| Space group | C2221 | P21 |
| Cell dimensions | ||
| a, b, c (Å) | 60.2, 84.7, 57.3 | 64.7, 59.5, 90.9 |
| α, β, γ (°) | 90, 90, 90 | 90, 101.7, 90 |
| Resolution (Å) | 1.2 | 3.1 |
| Rmerge | 0.051 (0.082) | 0.071 (0.372) |
| I/σI | 17.6 (6.0) | 18.8 (3.2) |
| Completeness (%) | 83.4 (45.0) | 99.9 (100) |
| Redundancy | 3.1(1.5) | 5.1(5.1) |
| Refinement | ||
| Resolution (Å) | 35–1.2 | 44–3.1 |
| No. reflections | 46 447 | 12 485 |
| Rwork/Rfree | 19.4/20.0 | 24.7/28.9 |
| No. atoms | ||
| Protein | 971 | 3655 |
| DNA | 874 | |
| Water | 175 | 2 |
| B-factors | ||
| Protein | 13.2 | 92.6 |
| DNA | 92.6 | |
| Water | 31.2 | 92.6 |
| Rmsd | ||
| Bond lengths (Å) | 0.010 | 0.004 |
| Bond angles (°) | 1.42 | 0.922 |
Figures in parentheses refer to values in the outer resolution shell. In the DNA complex structure the following residues are missing or have been truncated (indicated with *): M1, N15*, H20*, N21*, R66*, R67*, R68*, K101*, N119 and E120 from monomer A, M1, R19*, H20*, N21*, R22*, R24*, K43*, M46*, R66*, R68*, K76*, K101*, E116*, N119 and E120 from monomer B, M1, N2*, L8*, R16*, R19*, N21, R22, G23, R24, T25, H26, N37*, I41*, K43*, L47*, K56*, R67*, R68*, R69*, K76*, K84*, K101*, E116*, N119 and E120 from monomer C and M1, S13*, R16*, R19*, H20, N21, R22, G23, R24, R40*, I42*, K43*, R66*, R67*, R68*, K76*, K106*, R109*, N119 and E120 from monomer D. There are no residues missing or truncated in the structure of the free enzyme.