Table III.
Data Collection and Refinement Statistics for the hLon Proteolytic Domain
| 2.4 Å Data | 2 Å Data | |
|---|---|---|
| Data collection | ||
| Space group | P21 | P21 |
| Cell dimensions | ||
| a, b, c (Å) | 68.24, 82.96, 105.29 | 69.80, 83.75, 105.49 |
| α, β, γ (°) | 90, 89.97, 90 | 90, 90.05, 90 |
| Resolution (Å) | 2.39 (2.52−2.39) | 2 (2.11−2) |
| Rsym or Rmerge | 0.096 (0.566) | 0.063 (0.73) |
| I/σ (I) | 14.4 (3.2) | 10.9 (1.7) |
| Completeness (%) | 98 (96.7) | 99.4 (99.9) |
| Redundancy | 5.5 (5.2) | 3.6 (3.7) |
| Refinement | ||
| Resolution (Å) | 2.39 | 2 |
| No. reflections | 42,707 | 77,079 |
| Rwork/Rfree (%) | 20.85/26.16 | 19.36/23.23 |
| No. amino acid residues | 1098 | 1100 |
| No. atoms | ||
| Protein | 8296 | 8373 |
| Water | 155 | 330 |
| B-factors (Å2) | ||
| Protein | 47.0 | 50.5 |
| Water | 44.9 | 51.6 |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.009 (0.022) | 0.027 (0.022) |
| Bond angles (°) | 1.147 (1.970) | 2.095 (1.968) |
| Ramachandran plot (%) | ||
| Most favored | 91.9 | 94.5 |
| Additionally allowed | 7.9 | 5.5 |
| Generously allowed | 0.2 | 0 |
| Disallowed | 0 | 0 |
The numbers in brackets refer to the outer resolution shell. A single crystal was used for each data set. The following residues are disordered an omitted from the final model: chain A: 756–953, loop from 788–797; chain B: 756–948, loop from 784–798; chain C: 755–953, loop from 788–796; chain D: 760–948, loop from 785–797; chain E: 758–948, loop from 786–797; chain F: 759–948, loop from 785–797. For the data collection, the numbers in parentheses correspond to the outer shell of reflections. For the refinement deviations, the values in parentheses are the target values.