TABLE 1.
Data collection and refinement
| Zn2+ SADa | |
|---|---|
| Data collection | |
| Space group | P3221 |
| Cell dimensions | |
| a, b, c (Å) | |
| α, β, γ (°) | a = b = 90, γ = 120 |
| Resolution (Å)b | 50-2.9 (2.95-2.9) |
| Rsym (%)b,c | 9.7 (62) |
| I/σ(I)b | 46.2 (4.7) |
| Completeness (%)b | 99 (100) |
| Redundancyb | 14.9 (14.4) |
| Refinement | |
| Reflections used (all data) | 50.0-2.90 Å |
| Number of atoms | |
| Protein | 3306 |
| AdoMet | 54 |
| Zn2+ | 6 |
| Water | 27 |
| Total | 3393 |
| Rworkd (reflections) | 0.2348 (18,803) |
| Rfreed (reflections) | 0.2994 (963) |
| Ramachandran statistics | 69.5 (30.5) |
| r.m.s.e deviations | |
| Bond length (Å) | 0.009299 |
| Bond angle (°) | 1.73975 |
a SAD, single anomalous dispersion.
b Values in parentheses are for the highest-resolution shell.
c Rsym = Σ|(Ihkl − 〈Ihkl〉)|/(ΣIhkl), where 〈Ihkl〉 is the mean intensity of all reflections equivalent to the reflection hkl by symmetry.
d Rwork (Rfree) = Σ‖Fo| − |Fc‖/Σ|Fo|, where 5% of randomly selected data were used for Rfree.
e r.m.s., root mean square.