Table 1.
Data collection, phasing and refinement statistics
| SeMet | ||||
|---|---|---|---|---|
|
| ||||
| Data collection | ||||
| Space group | P21212 | |||
| Cell dimensions | ||||
| a, b, c (Å) | 151.97, 95.49, 100.36 | |||
| α, β, γ (°) | 90, 90, 90 | |||
| Peak | Inflection | Remote | ||
|
|
||||
| Wavelength | 0.9792 | 0.9793 | 0.9717 | |
| Resolution (Å) | 3.0 | 3.0 | 3.0 | |
| Rsym or Rmerge | 3.9 (11.1) | 4.0 (11.3) | 4.2 (12.5) | |
| I / σI | 19.1 (7.8) | 19.1 (7.8) | 17.9 (7.0) | |
| Completeness (%) | 99.9 (100.0) | 99.9 (100.0) | 99.9 (100.0) | |
| Redundancy | 9.8 (10.0) | 10.2 (10.4) | 9.9 (9.9) | |
| Refinement | SeMet | |||
| Resolution (Å) | 2.5 | |||
| No. reflections | 48059 | |||
| Rwork / Rfree | 23.2/26.8 | |||
| No. atoms | ||||
| Protein | 5985 | |||
| Ligand/ion | 0 | |||
| Water | 0 | |||
| B-factors | ||||
| Protein | 53.7 | |||
| Ligand/ion | ||||
| Water | ||||
| R.m.s deviations | ||||
| Bond lengths (Å) | 0.013 | |||
| Bond angles (°) | 1.1 | |||
*
A single SeMet crystal was used for both structure determination and refinement.
*
Values in parentheses are for highest-resolution shell.