Table 1.
Diffraction Data and Refinement Statistics
| RNase E Apoprotein | |
|---|---|
| Diffraction Data | |
| Space group | P1 |
| Unit cell dimensions | a = 73.24, b = 75.57, c = 109.37 Å |
| α = 94.95, β = 102.03, γ = 91.77° | |
| Resolution (Å) | 30.0−3.3 (3.42−3.30) |
| Number of unique reflections | 32,518 (3,144) |
| Multiplicity | 3.8 (3.2) |
| Completeness (%) | 98.1 (94.2) |
| I/σ | 11.8 (2.3) |
| Rmerge (%) | 10.8 (44.7) |
| Wilson B factor (Å2) | 70.6 |
| Refinement Statistics | |
| Resolution (Å) | 25.0−3.3 |
| R factor | 0.272 |
| Rfree | 0.294 |
| Number reflections used | 33,032 |
| Total number of atoms | 14,540 |
| Total number of amino acid residues | 1,954 |
Crystallographic statistics were calculated by use of Scalepack (Otwinowski and Minor, 1997) and SFCHECK (Vaguine et al., 1999). Refinement statistics were calculated by use of Refmac (Winn et al., 2001). All resolution shells were used for refinement of the apoprotein. No Ramachandran outliers are present.