Table 1.
Crystallographic information
| Data Collection | SeMet | Wild type |
|---|---|---|
| Space group | P21 | P21 |
| Cell Dimensions | ||
| a,b,c (Å) | 48.4, 130.4, 62.8 | 46.1, 129.1, 63.1 |
| α, β, γ (°) | 90, 112.0, 90 | 90, 111.5, 90 |
| X-ray Source | APS 23ID-D | APS 23ID-D |
| Wavelength (Å) | 0.979 | 1.033 |
| dmin (Å) | 2.09 (2.16–2.09)a | 2.10 (2.18–2.10) |
| R-merge | 0.1703 (1.492) | 0.1508 (1.048) |
| Inner-shell R-merge | 0.053 (9.3 Å)b | 0.049 (6.2 Å)b |
| Avg I/σ (I) | 11.62 (2.55) | 9.3 (1.37) |
| Completeness (%) | 100 (100) | 100 (100) |
| Multiplicity | 10.8 (10.4) | 6.6 (6.6) |
| Total observations | 463,157 (44,285) | 263,797 (26,230) |
| CC1/2 | 0.998 (0.683) | 0.997 (0.703) |
| CC* | 1 (0.901) | 0.999 (0.909) |
| Refinement | ||
| Data range (Å) | 44.48–2.09 | 43.43–2.10 |
| Reflections used in refinement | 42,794 | 39,893 |
| Rwork/Rfree (%) | 16.9/21.6 | 18.5/25.2 |
| Number of non-hydrogen atoms | 6355 | 6220 |
| macromolecules | 6049 | 6040 |
| ligands | 40 | 19 |
| water | 328 | 214 |
| Amino acid residues | 765 | 765 |
| Deviation from ideality | ||
| bond lengths (Å) | 0.003 | 0.007 |
| bond angles (°) | 0.60 | 0.92 |
| Average B-factor | 46.3 | 51.9 |
| protein | 46.0 | 52.0 |
| ligands | 86.3 | 70.3 |
| solvent | 46.8 | 44.5 |
| Ramachandran plot | ||
| favored (%) | 98 | 96 |
| allowed (%) | 2.5 | 3.4 |
| outliers (%) | 0 | 0.4 |
| PDB | 5THY | 5THZ |
a
Values in parentheses pertain to the outermost shell of data.
b
dmin inner shell