Table 2.
Crystallographic Statistics
| Crystal | Native | Hg |
|---|---|---|
| Space group | C2 | C2 |
| Cell lengths, Å | 63.8, 41.9, 48.7 | 63.5, 41.4, 48.4 |
| Cell angles, ° | 90, 107.5, 90 | 90, 106.9, 90 |
| X-ray data | ||
| Resolution (last shell) | 50–1.70 (1.76–1.70) | 50–1.81 (1.87–1.81) |
| Observations | 77,322 | 25,130 |
| Unique observations | 11,481 | 9,353 |
| Completeness, % (last shell) | 84.1 (30.9) | 84.6 (41.2) |
| Redundancy (last shell) | 6.7 (4.2) | 2.7 (1.9) |
| Rsym, % (last shell) | 5.0 (27.1) | 5.5 (25.1) |
| I/σI (last shell) | 40.0 (4.0) | 28.7 (3.2) |
| Phasing | ||
| No. of sites | 3 | |
| Phasing power acentric, centric | 2.26, 1.68 | |
| Figure of merit | 0.54 | |
| Figure of merit after DM | 0.74 | |
| Refinement | ||
| Rwork / Rfree, % | 16.7 / 20.6 | |
| No. of atoms | 1037 | |
| Protein | 883 | |
| Water | 154 | |
| B-factors, Å2 | ||
| Protein | 9.4 | |
| Water | 24.0 | |
| RMS deviations | ||
| Bonds (Å) | 0.009 | |
| Angles (°) | 1.239 |
The highest resolution shell is shown in parentheses.
Rsym = ΣhΣi|h,i-〈Ih〉 |/ΣhΣi|Ih,i| where Ih,i is the ith intensity measurement of reflection h and h 〈Ih〉 is the average intensity of that reflection.
Rwork / Rfree =Σh|FP-FC|/Σh|FP|, where FC is the calculated and FP is the observed structure factor amplitude of reflection h for the working or free set, respectively.