Table 3.
X-ray crystallographic data and refinement statistics for GltPh-R397A and GltPh-K55C-A364CHg structures not deposited at the PDB
| GltPh-R397A | GltPhin | ||
|---|---|---|---|
| Tl+-bound (apo conf.) | Tl+/Na+ (apo conf.) | Tl+/k+ (apo conf.) | |
| Data collection | |||
| Space group | P21 | C2221 | C2221 |
| Cell dimensions | |||
| a, b, c (Å) | 115.18, 428.53, 116.61 | 108.11, 198.86, 206.34 | 106.59, 198.48, 205.82 |
| α, β, γ (°) | 90.00, 119.49, 90.00 | 90.00, 90.00, 90.00 | 90.00, 90.00, 90.00 |
| Resolution (Å) | 30.0–5.0 (5.18–5.00) | 100.0–4.0 (4.07–4.00) | 100.0–4.15 (4.22–4.15) |
| Rsym or Rmerge | 10.9 (>100) | 15.0 (92.2) | 13.9 (94.1) |
| I/σI | 13.8 (1.9) | 8.9 (1.5) | 9.2 (1.5) |
| Completeness (%) | 86.4 (75.1) | 99.9 (100) | 94.5 (90.2) |
| Redundancy | 5.5 (5.8) | 3.9 (3.9) | 4.0 (3.9) |
| Refinement | |||
| Resolution (Å) | 20.0–5.0 | 15.0–4.0 | 15.0–4.15 |
| No. reflections | 34747 | 18184 | 15419 |
| Rwork/Rfree | 22.0/26.5 | 28.2/31.7 | 28.3/31.2 |
| No. atoms | |||
| Protein | 35107 | 9135 | 9135 |
| Ligand/ion | N/A | N/A | N/A |
| Water | N/A | N/A | N/A |
| B-factors | |||
| Protein | 223.00 | 183.6 | 194.4 |
| Ligand/ion | N/A | N/A | N/A |
| Water | N/A | N/A | N/A |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.008 | 0.006 | 0.008 |
| Bond angles (°) | 1.186 | 1.266 | 1.440 |