Table 1. Data collection and refinement statistics.
| Native | MMC-1a | MMC-2 | MMC-3 | HgAc | Se | |
|---|---|---|---|---|---|---|
| Data collection | ||||||
| Space group | P32 | P32 | P32 | P32 | P32 | P32 |
| Cell dimensions | ||||||
| a, b, c (Å) | 159.4, 159.4, 153.0 | 159.7, 159.7, 153.9 | 157.6, 157.6, 153.1 | 158.1, 158.1, 153.6 | 159.7, 159.7, 153.9 | 157.6, 157.6, 153.1 |
| α, β, γ (deg) | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 |
| Resolution (Å) | 40–3.6 (3.8–3.6)b | 40–4.6 (4.8–4.6) | 40–4.0 (4.1–4.0) | 40–4.5 (4.7–4.5) | 40–4.6 (4.8–4.6) | 40–5.0 (5.2–5.0) |
| Rmergec | 8.9 (67.5) | 9.3 (82.4) | 10.4 (76.1) | 16.0 (82.3) | 9.4 (50.2) | 10.9 (50.0) |
| I/σI | 9.0 (1.1) | 7.1 (1.1) | 8.8 (1.4) | 7.7 (1.0) | 8.5 (1.68) | 7.5 (2.0) |
| Completeness (%) | 93.8 (88.7) | 90.3 (90) | 97.7 (96.4) | 99.7 (99.0) | 96.4 (95.7) | 99.0 (99.0) |
| Redundancy | 2.0 (1.8) | 1.7 (1.7) | 3.2 (2.8) | 3.3 (3.0) | 2.4 (2.2) | 3.3 (3.1) |
| Refinement | ||||||
| Resolution (Å) | 19–3.6 (3.8–3.6) | |||||
| No of reflections | 47 021 | |||||
| Rwork/Rfree | 27.8 (35.8)/ 29.6 (40.4) | |||||
| No of protein atoms | 10 533 | |||||
| R.m.s. deviations | ||||||
| Bond lengths (Å) | 0.009 | |||||
| Bond angles (deg) | 1.12 | |||||
| aFor details on derivatisation see Supplementary Materials and methods. | ||||||
| bValues in parenthesis are for the highest-resolution shell. | ||||||
| cThe last shell Rmerge is high for some of the derivative data because of severe anisotropy in the diffraction images. | ||||||