Table 1.
X-ray data collection and refinement statistics
| TSTD1 | SeMet TSTD1 | |||
|---|---|---|---|---|
| Data collection | ||||
| Space group | P1 | P1 | ||
| Cell dimensions | ||||
| a, b, c (Å) | 37.9, 40.2, 47.2 | 38.1, 40.5, 47.5 | ||
| α, β, γ (degrees) | 113, 90, 117 | 113, 90, 117 | ||
| X-ray source | APS 23ID-B | APS 23ID-B | ||
| Wavelength (Å) | 0.7293 | 0.9793 | ||
| dmin (Å) | 1.04 (1.08 to 1.04)a | 1.26 (1.31 to 1.26)a | ||
| R-merge | 0.030 (0.698) | 0.055 (1.562) | ||
| Average I/σ(I) | 24.2 (1.7) | 18.31 (0.3) | ||
| Completeness (%) | 95.7 (89.7) | 81.08 (20.82) | ||
| Multiplicity | 7.0 (6.3) | 3.3 (1.9)b | ||
| Total observations | 703,631 (59,675) | 162,761 (3068)b | ||
| CC½ | 1 (0.908) | 0.998(0.257) | ||
| CC* | 1 (0.976) | 1 (0.64) | ||
| Refinement | ||||
| Data range (Å) | 23.28–1.04 | |||
| Reflections used in refinement | 100,881 (9498) | |||
| Rwork/Rfree (%) | 13.0/14.4 | |||
| Number of non-hydrogen atoms | 2494 | |||
| Protein | 1947 | |||
| Water | 547 | |||
| Amino acid residues | 227 | |||
| Deviation from ideality | ||||
| Bond lengths (Å) | 0.006 | |||
| Bond angles (degrees) | 0.98 | |||
| Average B-factor | 18.98 | |||
| Macromolecules | 15.51 | |||
| Solvent | 31.31 | |||
| Ramachandran plot (%) | ||||
| Favored | 97.3 | |||
| Allowed | 2.7 | |||
| Outliers | 0 | |||
| PDB code | 6BEV | |||
a Values in parentheses pertain to the outermost shell of data.
b Friedel pairs are kept separate for the anomalous wavelength data.