Table 3.
Crystal, Data Collection, and Phasing Statistics
| Crystal | |||
|---|---|---|---|
| Unit cell | a = b = 115.52 Å, c = 78.67 Å, α = β = 90°, γ = 120° | ||
| Space group | P3121 | ||
| MW (247 residues) Da | 28075 | ||
| Mol (AU) | 2 | ||
| SeMet (AU) | 22 | ||
| MAD Data Collection Statistics | |||
| λ1 (peak) | λ (inflection) | λ (remote) | |
| λ (Å) | 0.9791 | 0.9793 | 0.9639 |
| Resolution (Å) | 2.0 | 2.0 | 2.0 |
| Reflections (measured) | 328,134 | 288,593 | 234,067 |
| Reflections (unique) | 79,278 | 78,802 | 75,790 |
| Completeness (%) (outer shell) | 100 | 99.4 | 95.6 |
| Rmerge1 (overall) | 0.126 | 0.098 | 0.124 |
| I/σ (overall) | 19.4 | 19.4 | 9.3 |
| Number of selenium sites | 22 | 22 | 22 |
| Phasing power2 | 1.19 | 1.206 | 0.6265 |
| FOMMAD3 | 0.246 | 0.246 | 0.157 |
| FOMMAD (overall) | 0.442 | ||
| FOM (sf)4 | 0.824 | ||
1
Rmerge = ΣΣ | Ii – Im |/ ΣΣ Ii, where Ii is the intensity of the measured reflection and Im is the mean intensity of all symmetry-related reflections.
2
Phasing power = FH/ERMS.
FP, FPH, and FH are the protein, derivative, and heavy-atom structure factors, respectively, and ERMS is the residual lack of closure.
3
Figure of merit from MAD phasing.
4
Figure of merit after solvent flipping.