Table 2. Crystal data collection and refinement statistics.
Data restricted to highest resolution shell are shown in parentheses. All crystals were of the C619A mutant enzyme with His6 tag.
| GlcB complex with PDKA |
GlcB complex with 4 |
GlcB complex with 1 |
GlcB complex with 7 |
GlcB complex with 11 |
|
|---|---|---|---|---|---|
| Data collection | |||||
| Space group | P43212 | P43212 | P43212 | P43212 | P43212 |
| Cell dimensions | |||||
| a, b, c (Å) | 79.33, 79.33, 225.94 |
79.45, 79.45, 226.26 |
77.74, 77.74, 221.98 |
78.22, 78.22, 223.58 |
78.49, 78.49, 224.05 |
| a, b, g (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Resolution (Å) | 50-1.90 (1.93-1.9) |
43.05-1.80 (1.83-1.80) |
44.13-1.82 (1.92-1.82) |
49.57-2.04 (2.13-2.04) |
45.59-2.20 (2.24-2.20) |
| Rsym or Rmerge | 0.109 (0.532) | 0.191 (0.634) | 0.108 (0.554) | 0.099 (0.584) | 0.183 (0.742) |
| I/σI | 13.8 | 14.0 | 6.4 | 6.3 | 9.0 |
| Completeness (%) | 99.9 (99.4) | 97.2 (76.0) | 99.9 (100) | 99.2 (98.6) | 99.9 (100) |
| Redundancy | 13.1 (10.2) | 9.5 (2.6) | 9.7 (9.8) | 15.3 (15.4) | 14.4 (14.8) |
| Refinement | |||||
| Resolution (Å) | 50-1.90 | 43.05-1.8 | 44.13-1.82 | 49.57-2.04 | 45.59-2.2 |
| No. reflections | 57789 | 66563 | 62029 | 45023 | 36507 |
| Rwork/ Rfree | 0.1678/0.2027 | 0.1753/0.2192 | 0.1704/0.2196 | 0.1628/0.2040 | 0.1721/0.2231 |
| No. atoms | |||||
| Protein | 5543 | 5645 | 5562 | 5509 | 5429 |
| Ligand/ion | 14/3 | 15/3 | 15/3 | 15/3 | 17/3 |
| Water | 674 | 859 | 641 | 574 | 400 |
| B-factors | |||||
| Protein | 27.86 | 29.64 | 21.22 | 32.13 | 34.69 |
| Ligand/ion | 30.47/28.14 | 20.7/32.13 | 14.24/27.53 | 30.1/38.4 | 28.87/39.3 |
| Water | 39.65 | 40.55 | 28.79 | 38.58 | 40.78 |
| R.m.s deviations | |||||
| Bond lengths (Å) | 0.013 | 0.007 | 0.007 | 0.007 | 0.008 |
| Bond angles (°) | 1.03 | 1.024 | 1.013 | 1.013 | 1.062 |