Table I. Data collection, phasing and refinement statistics.
| 12S–MMCoA–Cda | 12S–CoA–Cda | 12S–CoA–Cd–Hga | 12S–CoA | |
|---|---|---|---|---|
| Data collection |
|
|
|
|
| Space group | C2 | C2 | C2 | C2 |
| Unit cell (Å3) | 114.8 × 200.7 × 146.3 | 113.8 × 200.0 × 145.9 | 115.2 × 201.1 × 146.5 | 115.5 × 201.4 × 146.9 |
| β (°) | 102.4 | 102.97 | 102.4 | 102.7 |
| Wavelength (Å) | 1.04 | 1.00 | 1.54 | 1.00 |
| Resolution (Å) | 20–1.9 (1.97–1.9) | 30–1.9 (1.97–1.9) | 100.0–2.8 (2.9–2.8) | 30–2.1 (2.18–2.1) |
| <I>/<σ(I)> | 15.6 (3.6) | 20.0 (4.9) | 22.3 (5.2) | 16.0 (1.9) |
| Rmerge (%) | 5.7 (26.8) | 5.5 (23.6) | 7.3 (18.7) | 6.5 (34.7) |
| Completeness (%) |
95.4 (97.4) |
92.6 (69.1) |
93.4 (86.7) |
90.2 (58.2) |
| MIR phasing |
|
|
|
|
| Resolution (Å) | 30–2.8 | 30–2.8 | ||
| Number of sites | 3 Cd | 3 Cd | 12 Hg, 3 Cd | |
| Rcullis | 0.86 | 0.871 | ||
| Phasing power | 0.98 | 0.99 | ||
| Mean f.o.m. |
|
|
0.267 (MIRAS) |
0.649 (after DM) |
| Refinement |
|
|
|
|
| Resolution (Å) | 20–1.9 | 30–2.0 | ||
| Rwork, Rfree | 0.168, 0.213 | 0.152, 0.198 | ||
| R.m.s.d. | ||||
| Bond lengths (Å) | 0.0079 | 0.0080 | ||
| Bond angles (°) | 1.41 | 1.50 | ||
| B-factor, mean (Å2) | ||||
| Protein | 21.5 | 19.1 | ||
| Substrate | 36.0 | 77.7 | ||
| Ions | 16.4 | 13.8 | ||
| Other heteroatoms | 42.4 | 25.2 | ||
| Solvent | 33.9 | 31.6 | ||
| R.m.s.d., bonded | 2.4 | 2.3 | ||
| R.m.s.d., angled | 2.9 | 2.8 | ||
| Ramachandran (%) | ||||
| most favored, disallowed | 89.6, 0.0 | 90.0, 0.1 |
Values in parentheses are for the highest resolution shell.
aFor MIRAS phasing, the 12S–CoA–Cd data set was used as native, 12S–CoA as derivative 1 (with negative occupancies) and 12S–CoA–Cd-Hg as derivative 2.