Table 1.
X-ray crystallography data collection and refinement statistics.
| AgIMPDH-ATP | AgIMPDH_ATP/GDP | |
|---|---|---|
| Data collection | ||
| Space group | P21 | I4 |
| Cell dimensions | ||
| a, b, c (Å) | 127.89, 152.09, 152.26 | 147.88, 147.88, 103.54 |
| α, β, γ (°) | 90.00, 93.03, 90.00 | 90.00, 90.00, 90.00 |
| Resolution (Å) | 127.7–2.40 (2.49–2.40) | 46.76–2.46 (2.55–2.46) |
| R merge | 0.21 (1.36) | 0.14 (1.44) |
| I/σI | 5.8 (1.3) | 10.64 (1.4) |
| Completeness (%) | 99.8 (99.3) | 99.78 (99.3) |
| Redundancy | 6.5 (6.3) | 13.1 (13.5) |
| Refinement | ||
| Resolution (Å) | 2.4 | 2.5 |
| No. reflections | 226311 (22460) | 40435 (4028) |
| R-work | 0.2511 (0.3171) | 0.2270 (0.4035) |
| R-free | 0.2729 (0.3421) | 0.2462 (0.4292) |
| No. atoms | ||
| Protein | 22502 | 7218 |
| Ligand/ion | 752 | 234 |
| Water | 1277 | 51 |
| B-factors | ||
| Protein | 71.39 | 75.80 |
| Ligand/ion | 81.58 | 68.76 |
| Water | 48.66 | 59.40 |
| R.m.s deviations | ||
| Bond lengths (Å) | 0.015 | 0.014 |
| Bond angles (°) | 1.68 | 1.26 |
Statistics for the highest-resolution shell are shown in parentheses. Friedel mates were averaged when calculating reflection statistics. Data for both structures were collected using a single crystal.