Table 1.
Scaling and Model-Building Statistics of the TPRL254F Crystal Structure
| TPRL254F | |
|---|---|
| Data Collection | |
| Space group | C2221 |
| Cell dimensions | |
| α, β, γ (°) | 44.00, 203.16, 116.87 |
| a, b, c (Å) | 90.00, 90.00, 90.00 |
| Resolution (Å) | 46.58–1.75 (1.75–1.78) |
| Rsym or Rmerge | 0.05 (0.57) |
| I/σI | 13.00 (2.00) |
| Completeness (%) | 99.70 (99.80) |
| Redundancy | 4.1 (4.1) |
| Refinement | |
| Resolution (Å) | 46.58–1.75 (1.75–1.78) |
| No. of reflections | 54,404 (3,607) |
| Rwork/Rfree | 0.19/0.23 |
| No. of atoms | 3,002 |
| Protein | 2,722 |
| Ligand/ion | NA |
| Water | 280 |
| B factors | |
| Protein | 38.40 |
| Ligand/ion | NA |
| Water | 42.52 |
| RMSDs | |
| Bond lengths (Å) | 0.02 |
| Bond angles (°) | 2.00 |
Related to Figures 1C and 1D. Values in parentheses represent the highest-resolution shell.