Table 1.
Crystallographic data collection and refinement statistics
| T686A:Quis | T686A:Glu | T686S:Glu | |
|---|---|---|---|
| Data collection | |||
| Space group | C2 | C2 | P21 |
| Cell dimensions | |||
| a, b, c (Å) | 123.0, 47.2, 49.9 | 123.2, 47.3, 49.7 | 47.8, 95.8, 122.9 |
| α, β, γ (°) | 90, 110.8, 90 | 90, 110.6, 90 | 90, 93.43, 90 |
| Resolution (Å) | 2.1 (2.21–2.10) | 2.0 (2.11–2.00) | 1.7 (1.79–1.70) |
| Rsym or R merge | 0.073 (0.276)a | 0.080 (0.295) | 0.059 (0.297) |
| I/σI | 8.3 (2.3) | 8.8 (2.6) | 6.6 (2.3) |
| Completeness (%) | 98.0 (97.1) | 97.6 (97.6) | 98.3 (95.9) |
| Redundancy | 3.3 (3.3) | 3.5 (3.5) | 3.4 (3.4) |
| Refinement | |||
| Resolution (Å) | 2.1 | 2.0 | 1.7 |
| Number of reflections | 14,748 | 17,201 | 113,281 |
| Rwork/Rfree | 0.21/0.27 | 0.18/0.22 | 0.23/0.26 |
| Number of atoms | |||
| Protein | 1962 | 1963 | 7790 |
| Ligand | 13 | 10 | 20 |
| Ion | 5 | 5 | 20 |
| Water | 157 | 151 | 596 |
| B factors | |||
| Protein | 15.3 | 16.4 | 21.4 |
| Ligand | 10.8 | 10.9 | 12.4 |
| Ion | 28.2 | 24.8 | 35.4 |
| Water | 19.5 | 21.3 | 25.3 |
| RMS deviations | |||
| Bond lengths (Å) | 0.025 | 0.017 | 0.014 |
| Bond angles (°) | 2.234 | 1.552 | 1.438 |
A single dataset collected from a single crystal was used for each structure. There was one molecule in the asymmetric unit of the glutamate or quisqualate–T686A complex and four molecules in the glutamate–T686S complex. RMS, Root mean square.
aHighest resolution shell is shown in parentheses.