Table 1.
X-ray data collection and refinement statistics
| Variable | Value |
| Data collection | |
| Space group | P21 |
| Cell dimensions | |
| a, b, c | 46.86, 82.39, and 83.40Å |
| α, β, γ | 90, 95.2, and 90° |
| Wavelength | 0.9790 |
| Resolution | 50.0–2.35Å |
| Rsym or Rmerge | 5.9 (27.5)a |
| I/σI | 19 (3.2)a |
| Completeness | 91.7% (98.3%)a |
| Redundancy | 2.9 |
| Refinement | |
| Resolution | 2.35Å |
| No. reflections | 22,885 |
| Rwork/Rfree | 23.0/27.5 |
| Number of atoms | |
| Protein | 4,004 |
| Solvent | 260 |
| B factors | |
| Protein | 17.5 |
| Solvent | 21.2 |
| R.m.s deviations | |
| Bond lengths | 0.006Å |
| Bond angles | 0.88° |
a
Values in parentheses are for the highest resolution shell (2.35–2.41 Å). One crystal was used for each data set. TLS (translation/libration/screw) parameters, one set for each protomer, were included in the refinement.