Table 1. Data collection, phasing and refinement statistics for Myo5a globular domain (MAD).
| Native | Selenomethionine | ||
| Data collection | |||
| Space group | P212121 | P3221 | |
| Cell dimensions | |||
| a, b, c (Å) | 74.06, 87.11, 130.94 | 146.92, 146.92, 200.00 | |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 120 | |
| Peak | Inflection | ||
| Wavelength | 0.9334 | 0.9785 | 0.9790 |
| Resolution (Å) | 43.5–2.2 (2.3–2.2) | 49.3–2.5 (2.6–2.5) | 49.3–2.5 (2.6–2.5) |
| R sym or R merge | 9.3 (48.3) | 9.4 (25.6) | 10.5 (31.3) |
| I/σI | 18.4 (5.0) | 16.3 (7.5) | 15.3 (6.4) |
| Completeness (%) | 99.6 (99.5) | 100 (99.3) | 100 (94.9) |
| Redundancy | 7.3 (7.5) | 11.3 (11.5) | 11.3 (11.5) |
| Phasing power | 2.15 (for 48.0–2.8 Å) | ||
| Figure of merit | 0.48 (for 48.0–2.8 Å) | ||
| Refinement | |||
| Resolution (Å) | 43.5–2.2 | 49.3–2.5 | 49.3–2.5 |
| No. reflections | 43,514 | ||
| R work/R free | 21.5/25.6 | ||
| No. atoms | |||
| Protein | 6,493 | ||
| Water | 427 | ||
| B-factors | |||
| Protein | 29.4 | ||
| Water | 12.4 | ||
| R.m.s deviations | |||
| Bond lengths (Å) | 0.0136 | ||
| Bond angles (°) | 1.04 | ||
*
Values in parentheses are for highest-resolution shell.