Table 2. Crystallographic data collection and refinement statistics.
| Nterm2 | Nterm2 + Trypsin | |
| Data Collection | ||
| Wavelength (Å) | 1.5417 | 0.9786 |
| Space Group | P1 21 1 | P31 2 1 |
| Unit Cell Dimensions (Å) | 32.51, 27.03, 56.83 | 57.39, 57.39, 105.31 |
| Unit Cell Angles (°) | 90.0, 94.3, 90.0 | 90.0, 90.0, 120.0 |
| Resolution (Å)a | 32.42–1.73 (1.82–1.73) | 52.65–2.04 (2.15–2.04) |
| R-merge | 0.092 (0.308) | 0.096 (0.562) |
| Completeness (%) | 99.4 (96.3) | 100.0 (100.0) |
| Redundancy | 9.77 (9.18) | 20.43 (20.45) |
| No. of Observations | 102957 (13617) | 272612 (38858) |
| No. of Unique Reflections | 10538 (1483) | 13341 (1900) |
| Mean I/σ(I) | 17.1 (6.9) | 22.6 (6.2) |
| Refinement | ||
| R-factor | 0.160 (0.195) | 0.251 (0.283) |
| R-free | 0.185 (0.253) | 0.287 (0.337) |
| Cruickshanks DPI (Å) | 0.114 | 0.179 |
| Protein Atoms | 834 | 838 |
| Solvent Atoms | 206 | 135 |
| Average B-value (Å2) | 13.6 | 36.7 |
| RMSD | ||
| Bond Angles (°) | 0.914 | 0.997 |
| Bond Lengths (Å) | 0.006 | 0.008 |
a
Numbers in parentheses correspond to the highest resolution shell.