Table 2. Crystallographic data collection and refinement statistics.
| Wild-type | SENK312A | SENK362A | |
|---|---|---|---|
| Data collection | |||
| Space group | P4 | P4 | P4 |
| Cell dimensions | |||
| a, b, c (Å) | 185.8, 185.8, 56.3 | 181.6, 181.6, 56.4 | 187.3, 187.3, 57.2 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Resolution (Å) | 19.75–2.90 (3.00–2.90) a | 90.81–2.15 (2.23–2.15) a | 19.97–2.1 (2.17–2.10) a |
| R meas | 0.432 (1.127) | 0.241 (1.206) | 0.149 (1.5) |
| <I / σ(I)> | 4.60 (1.91) | 10.64 (2.13) | 14.16 (2.10) |
| Completeness (%) | 99.69 (98.83) | 99.99 (100.00) | 100.00 (100.00) |
| Multiplicity | 6.0 (5.0) | 11.8 (10.1) | 11.3 (7.1) |
| Twin fraction | 0.460 | 0.134 | 0.109 |
| Refinement | |||
| Resolution (Å) | 2.9 | 2.15 | 2.10 |
| No. unique reflections | 43076 (4208) | 100879 (10040) | 116292 (11538) |
| R work / R free | 0.153 / 0.205 | 0.173 / 0.199 | 0.179 / 0.207 |
| No. atoms | |||
| Protein | 13172 | 13919 | 13704 |
| Ligand/ion | 0 | 40 | 40 |
| Water | 0 | 577 | 424 |
| Average B-factors | |||
| Protein | 52.87 | 40.06 | 39.41 |
| Ligand/ion | - | 47.06 | 64.58 |
| Water | - | 30.51 | 33.64 |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.016 | 0.005 | 0.006 |
| Bond angles (°) | 1.730 | 0.866 | 0.926 |
a Each dataset was collected from a single crystal; the values in parentheses are for the highest-resolution shell. R meas = ∑ hkl(N(hkl)/[N(hkl)-1])1/2 ∑i|Ii(hkl)- <I(hkl)>|/ ∑hkl∑iIi(hkl), where I i(hkl) is the intensity of the ith measurement of an equivalent reflection with indices hkl.