Table 1.
Data collection, phasing and refinement statistics
| native | Hg derivative | Pt derivative | |
|---|---|---|---|
| Data collection | |||
| Space group | P21 | P21 | P21 |
| Cell dimensions | |||
| a, b, c (Å) | 95.13,248.54, 103.46 | 95.04,248.99, 102.34 | 94.86,248.76, 103.74 |
| β (°) | 106.94 | 106.59 | 107.17 |
| Resolution (Å)* | 40–3 (3.11–3) | 40–4.2 (4.35–4.2) | 40–4.2 (4.35–4.2) |
| Unique reflections | 85645 | 29275 | 301365 |
| Rmerge | 0.079 (0.430) | 0.148 (0.289) | 0.065 (0.126) |
| I/σ(I) | 21.2 (3.8) | 10.3 (5.5) | 29.2 (14.9) |
| Completeness(%) | 93.0 (90.4) | 88.4 (86.2) | 93.9 (91.1) |
| Redundancy | 2.6 (2.1) | 2.1 (2.0) | |
| MIR phasing | |||
| Resolution (Å) | 25–4 | 25–4.2 | 25–4.2 |
| Riso* | 0.245 | 0.144 | |
| Rcullis* (acentric/centric)* | 0.84/0.79 | 0.87/0.89 | |
| Phasing power* (acentric/centric) | 1 .22/0.96 | 0.96/0.87 | |
| Combined figure of merit* | 0.361 | ||
| Refinement | |||
| Resolution (Å) | 30–3 | ||
| No. reflections | 83574 | ||
| Rwork/Rfree | 0.257/0.281 | ||
| No. atoms | |||
| Protein | 17096 | ||
| Water | 61 | ||
| B-factors (Å2) | 60.4 | ||
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.011 | ||
| Bond angles (°) | 1.6 | ||
| Ramachandran plot | |||
| Favored (%) | 80.6 | ||
| Allowed (%) | 18.9 | ||
| Generous (%) | 0.6 | ||
| Disallowed (%) | 0 | ||
*
Number of shells is 10 for each structure. Values in parentheses are for highest-resolution shell. Riso = Σhkl| FPH − Fp|/ΣhklFp; Rcullis = Σhkl| FPH − |Fp ± FH(calc)||/ΣhklFPH− FP|; Phasing power = 〈FH(calc)〉/〈FPH −|FP ±/FH(calc)| 〉, where FPH and FP are the structure-factor amplitudes of the derivative and native crystals, respectively, and FH(calc) is the calculated heavy atoms structure-factor amplitude.