Table 1.
Data Collection and Refinement Statistics
| Data Collection Statistics
| ||
|---|---|---|
| Peak (λ = 1.2831 Å) | Inflection Point (λ = 1.2837 Å) | |
| Space group and unit cell (Å) | P3121a = b = 115.3 c = 106.4 | |
| Resolution (Å)a | 50.0–1.97 (2.05–1.97) | 30.0–1.97 (2.05–1.97) |
| Total reflections | 460,699 | 543,743 |
| Unique reflections | 124,827 (12,464) | 124,854 (12,466) |
| Redundancy | 3.7 (3.7) | 4.4 (4.3) |
| Completeness (%)a | 100 (100) | 100 (100) |
| Rsyma,b (%) | 5.0 (51.2) | 4.2 (35.2) |
| I/σ (I)a,b | 24.57 (2.64) | 34.7 (4.1) |
|
| ||
| Phasing Statistics
| ||
| Resolution (Å) | 50.0–2.50 | |
| Anomalous phasing power acentricc | 0.34 | |
| Anomalous Rcullisd | 0.81 | |
| Figure of merit | 0.28 | |
|
| ||
| Refinement Statistics
| ||
| Resolution (Å) | 20.0–1.97 | |
| Reflections (working) | 56,615 | |
| Reflections (test) | 1,186 | |
| Rwork (%)e | 19.7 | |
| Rfree (%)e | 22.4 | |
| Number of protein atoms | 4,382 | |
| Number of waters | 277 | |
| Number of acetate ions | 6 | |
| Number of Zn ions | 2 | |
| Rms deviations | ||
| Bond lengths (Å) | 0.025 | |
| Bond angles (°) | 1.849 | |
| Average B factor (Å2) | ||
| Main chain | 36.0 | |
| Side chain | 40.6 | |
| Waters | 39.2 | |
Values in parentheses correspond to the last shell.
Rsym = Σ|Ii − <I>|/ΣI, where Ii is the intensity of the i-th observation, and <I> is the mean intensity of the reflections. The values are for unmerged Friedel pairs.
Phasing power = rms (|Fh|/E), where |Fh| is the heavy atom structure factor amplitude, and E is residual lack of closure error.
Rcullis = Σ||Fh.obs| − |Fh.calc||/Σ|Fh| for acentric reflections, where |Fh.obs| is the observed heavy atom structure factor amplitude, and |Fh.calc| is the calculated heavy atom structure factor amplitude.
Rwork = Σ||Fobs| − |Fcalc||/Σ|Fobs|, crystallographic R factor, and Rfree = Σ||Fobs| − |Fcalc||/Σ|Fobs|, where all reflections belong to a test set of randomly selected data.