Table 2.
Data collection, phasing and refinement statistics
| Native | Se | Pt | ||||
|---|---|---|---|---|---|---|
| Data collection | ||||||
| Space group | P212121 | P212121 | ||||
| Cell dimensions | ||||||
| a, b, c (Å) | 41.0, 76.7, | 41.14, 77.06, | 40.6, 76.2 | |||
| 126.5 | 126.8 | 128.4 | ||||
| α, β,γ (°) | 90 90 90 | 90 90 90 | 90 90 90 | |||
| Inflection | Remote | Peak | Inflection | Remote | ||
| Wavelength | 1.072 Å | 0.9794 Å | 0.9686 Å | 1.072 Å | 1.054 Å | 1.5418 Å |
| Resolution (Å) | 2.1 | 3.0 | 3.0 | 2.5 | 2.7 | 2.6 |
| Rsym or Rmerge | 4.3 (34.7) | 7.5 (14.1) | 7.6 (10.1) | 8.1 (21.9) | 6.9 (22.8) | 6.9 (50.4) |
| I/σI | 21.3 | 16.0 | 13.8 | 13.4 | 14 | 18.3 |
| Completeness (%) | 92.2 (81.8) | 96.5 (89.1) | 97.4 (75.6) | 98.5 (96.1) | 98.9 (97.0) | 98.1 (87.5) |
| Redundancy | 7 | 10 | 11 | 8 | 4 | 13 |
| Refinement | ||||||
| Resolution (Å) | 2.1 | |||||
| No. reflections | 21275 | |||||
| Rwork/Rfree | 23.4/28.5 | |||||
| No. atoms | ||||||
| Protein | 2380 | |||||
| Ligand/ion | 6 | |||||
| Water | 89 | |||||
| B-factors | ||||||
| Protein | 65.765 | |||||
| Ligand/ion | 75.9 | |||||
| Water | 63.85 | |||||
| R.m.s deviations | ||||||
| Bond lengths (Å) | 0.008 | |||||
| Bond angles (°) | 1.37 | |||||
*
Three crystals are used for structure solving and refinement *Highest-resolution shell is shown in parentheses.