TABLE 1.
Crystallographic data, phasing, and refinement statistics
| Data collection and phasing | 16-286 | SeMet |
|---|---|---|
| Space group | P3221 | P3221 |
| Unit cell | a = b = 130.8 Å, c = 129.9 Å; α = β = 90°, γ = 120° | a = b = 130.2 Å, c = 129.4 Å; α = β = 90°, γ = 120° |
| Wavelength (Å) | 1.000 | 0.97166 |
| Resolution (Å) | 46-2.9 | 50-3.1 |
| Unique reflections | 28,738 | 44,459 |
| Completeness (%) | 100 (100)a | 100 (100) |
| Rmergeb | 8.5 (52.4) | 9.2 (52.6) |
| FOM (SAD) | 1.31 | |
| Refinement | ||
| Resolution range (Å) | 46–2.9 (2.975–2.90) | |
| No. of reflections | 314,752 (43,621) | |
| R (%) | 23.64 (31.5) | |
| Rfree (%) | 24.61 (37.0) | |
| r.m.s.d.c | ||
| Bond length (Å) | 0.015 | |
| Bond angle | 1.496° | |
| B factor (Å2) main chain bonds | 0.917 | |
| B factor (Å2) side chain bonds | 2.725 | |
| Protein atoms, number | 3444 | |
| Ligand atoms, number | 30 | |
| Residues in allowed ϕ-ψ region | 99.5% | |
a Data in parentheses are for highest resolution shells.
b Rsym = Σhkl√(N/(N − 1))Σi|Ii(hkl) − 〈I(hkl)〉|/ΣiIi(hkl).
c r.m.s.d., root mean square deviation.