Table 1.
Data collection and refinement statistics
| Statistic | HMGS·apo | HMGS·F-244 | HMGS·Ac-CoA | HMGS·HMG-CoA* |
|---|---|---|---|---|
| Data collection | ||||
| Space group | P6(1)22 | P6(1)22 | P6(1)22 | P6(1)22 |
| Cell dimensions | ||||
| a, b, c, Å | 61.27, 61.27, 435.70 | 61.04, 61.04, 411.77 | 61.34, 61.34, 409.87 | 61.19, 61.19, 410.93 |
| α, β, γ, ° | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 |
| Resolution, Å | 50–2.1 (2.22–2.1) | 50–2.5 (2.65–2.50) | 50–2.5 (2.66–2.5) | 50–2.49 (2.64–2.49) |
| Rsym or Rmerge | 6.7 (28.4) | 10.0 (40.0) | 11.3 (48.9) | 13.0 (62.1) |
| I/σI | 20.16 (4.82) | 19.93 (4.90) | 16.26 (3.10) | 17.46 (3.04) |
| Completeness, % | 98.0 (89.5) | 96.8 (83.4) | 97.4 (85.6) | 96.7 (86.4) |
| Redundancy | 8.05 | 11.6 | 7.9 | 13.4 |
| Refinement | ||||
| Resolution, Å | 2.1 | 2.5 | 2.5 | 2.5 |
| No. reflections | 27,963 | 15,746 | 15,876 | 16,104 |
| Rwork/Rfree | 0.19/0.24 | 0.17/0.24 | 0.19/0.28 | 0.19/0.24 |
| No. atoms | ||||
| Protein | 3,510 | 3,510 | 3,510 | 3,510 |
| Ligand/ion | 0 | 22 | 53 | 57, 57* |
| Water | 154 | 272 | 133 | 99 |
| B factors | ||||
| Protein | 34.15 | 23.64 | 30.97 | 29.36 |
| Ligand/ion | 30.32 | 48.23 | 31.84 | |
| Water | 37.88 | 28.01 | 33.00 | 26.13 |
| rmsd | ||||
| Bond lengths, Å | 0.015 | 0.011 | 0.014 | 0.021 |
| Bond angles, ° | 1.55 | 1.35 | 1.55 | 2.29 |
One crystal was used for each structure summarized above. Numbers in parentheses represent the highest-resolution shell.
*Two ligands of the same size refined with the occupancy of each set to 50%.