Table 1.
Data measurement and structure refinement statistics
| Pimelate/succinyl-CoA | L-2-aminopimelate/ succinamide-CoA | |
| Data measurement | ||
| Resolution (Å) | 2.3 | 2.0 |
| Observed reflections | 47749 | 59293 |
| Unique reflections | 11389 | 16693 |
| Redundancy | 4.3 | 3.5 |
| Rmerge (%)a,b | 7.2 (33.9) | 4.8 (21.7) |
| 〈I/σI〉 | 21.3 (3.6) | 20.8 (3.2) |
| Completeness (%)c | 99.8 (99.9) | 99.5 (97.9) |
| Atoms | ||
| Protein atoms | 2078 | 2079 |
| Substrate atoms | 11/55 | 12/55 |
| Water molecules | 59 | 87 |
| RMS deviation from ideality | ||
| Bond lengths (Å) | 0.024 | 0.022 |
| Bond angles (°) | 2.2 | 2.2 |
| Average thermal factors (Å2) | ||
| Protein atoms | 33.9 | 27.7 |
| Substrate/cofactor atoms | 24.2/40.4 | 13.8/32.8 |
| Solvent atoms | 42.1 | 42.3 |
| Rfree (%)d | 26.1 (35.0) | 25.0 (34.1) |
| Rfactor (%)e | 17.1 (26.0) | 17.9 (27.0) |
a Rmerge (%) = ∑| Ii − |∑| Ii | × 100 where Ii is an individual intensity observation, ≤I> is the mean intensity for that reflection and the summation is over all reflections.
b Numbers in parentheses refer to the highest resolution shell: pimelate/succinyl-CoA, 2.50 − 2.30 Å; L-2-aminopimelate/succinamide-CoA, 2.10 − 2.00 Å.
c Completeness is the ratio of the number of observed unique reflections to the total number of theoretically possible reflections × 100.
d Rfree (%) = ∑ | Fo − Fc | /∑ | Fo | × 100 for a 5% subset of X-ray diffraction data omitted from refinement calculations.
e Rfactor (%) = ∑ | Fo − Fc | /∑∼ | Fo | × 100 for all available data.