Table I.
Statistics of Data Collection and Refinement
| Data sets | Native | Hg-SAD |
|---|---|---|
| Diffraction data | ||
| Wavelength (Å) | 1.0000 | 1.0064 |
| Resolution (Å) | 50–1.9 | 50–2.2 |
| Measured reflections | 313,879 | 361,298 |
| Unique reflections | 11,404 | 7,433 |
| Completeness (%) | 100 (100) | 99.9 (99.7) |
| Average (I/σ) | 67.1 (12.1) | 15.4 (2.2) |
| Rsym (%) | 10.1 (36.9) | 10.6 (34.7) |
| Phasing | ||
| Overall figure of merit (50–2.4 Å) | 0.30 | |
| Refinement | ||
| Resolution range (Å) | 30–1.9 | |
| Number of reflections | 11,126 | |
| Rworking (%) | 21.7 | |
| Rfree (%) | 23.8 | |
| Number of water molecules | 94 | |
| RMS deviation bond length (Å) | 0.006 | |
| RMS deviation bond angles (Å) | 1.1 | |
Rsym = ΣhΣi|Ih,i – Ih|/ΣhΣIIh,i, where Ih is the mean intensity of the i observations of symmetry-related reflections of h. R = Σ|Fobs – Fcalc|/ΣFobs, where Fobs = Fpi and Fcalc is the calculated protein structure factor from the atomic model (Rfree was calculated with 5% of the reflections). RMS deviation in bond lengths and angles are the deviations from ideal values, and the RMS deviation in B factors is calculated between bonded atoms.