Table 1.
Crystallographic data collection and refinement statistics
| Structure | MdcD–MdcE hetero-dimer | MDC hetero-tetramer | MDC hetero-tetramer |
|---|---|---|---|
| Malonate complex | CoA complex | ||
| Data collection | |||
| Space group | P1 | P1 | P21 |
| Cell dimensions | |||
| a, b, c (Å) | 56.3, 60.1, 91.3 | 93.5, 161.4, 102.7 | 98.7, 163.6, 100.4 |
| α, β, γ (°) | 89.9, 88.8, 68.8 | 90.8, 93.8, 90.1 | 90, 94.0, 90 |
| Resolution (Å)a | 46–1.86 (1.92–1.86) | 50–2.2 (2.28–2.2) | 50–3.0 (3.18–3.0) |
| R merge (%) | 6.2 (38.6) | 7.2 (45.7) | 10.0 (67.9) |
| CC1/2 | – | – | 99.4 (72.1) |
| I/σI | 12.7 (2.5) | 9.6 (1.6) | 12.0 (1.7) |
| Completeness | 96.0 (92.6) | 97.4 (95.3) | 98.8 (97.9) |
| Redundancy | 3.1 (3.0) | 1.9 (1.8) | 3.2 (3.3) |
| Refinement | |||
| Resolution (Å) | 46–1.86 (1.90–1.86) | 50–2.2 (2.23–2.2) | 50–3.0 (3.04–3.0) |
| No. reflections | 88,297 | 294,062 | 63,159 |
| R work/R free (%) | 18.1 (22.6)/20.8 (25.0) | 18.6 (27.3)/23.2 (33.1) | 17.3 (32.9)/23.3 (39.0) |
| No. atoms | |||
| Protein | 7474 | 35,976 | 18,104 |
| Ligand/ion | 0 | 28 | 97 |
| Water | 216 | 1459 | 0 |
| B-factors | |||
| Protein | 23.9 | 36.2 | 64.6 |
| Ligand/ion | – | 27.8 | 67.1 |
| Water | 24.8 | 34.8 | – |
| rms deviations | |||
| Bond lengths (Å) | 0.008 | 0.009 | 0.010 |
| Bond angles (°) | 1.0 | 1.2 | 1.5 |
| PDB entry code | 5VIP | 5VIT | 5VJ1 |
aThe numbers in parentheses are for the highest resolution shell