Table 2. Comparison of crystallographic statistics for different analysis methods.
| Method | Serial Laue (this work) | Microfluidic and monochromatic (Perry et al., 2013 ▶) | Cryo and monochromatic (Perry et al., 2013 ▶) |
|---|---|---|---|
| Protein | Native | SeMet | SeMet |
| Number of crystals | 58 | 19 | 1 |
| Frames per crystal | 1 | 10 | 360 |
| Resolution () | 502.09 | 502.11 | 502.09 |
| Unique observations | 26001 | 28002 | 27839 |
| Total observations | 392174 | 412491 | 809937 |
| Redundancy† | 44.8 (1.0) | 7.9 (6.7) | 29.1 (29.4) |
| R merge on F 2 | 0.119 | ||
| R merge on F | 0.083 | ||
| R sym | 0.111 (0.508) | 0.062 (0.145) | |
| Mean F/(F)† | 29.3 (6.1) | 15.4 (6.6) | 58.7 (32.6) |
| Completeness (%)† | 89.7 (45.8) | 99.8 (99.8) | 100 (100) |
| Structure refinement | |||
| R, R free | 0.195, 0.245 | 0.176, 0.211 | 0.149, 0.184 |
| Favored residues | 376 (92.8%) | 392 (95.6%) | 382 (94.3%) |
| Allowed residues | 23 (5.7%) | 11 (2.7%) | 19 (4.7%) |
| Disallowed residues | 6 (1.5%) | 7 (1.7%) | 4 (1.0%) |
†
Numbers in parentheses are for the high-resolution shell.