Table 1.
X-ray data and refinement statistics
| A. aeolicus TrmI | |
|---|---|
| Crystal parameters | |
| Space group | P 21 21 21 |
| Cell dimensions | |
| a, b, c (Å) | 69.8, 97.2, 212.7 |
| α, β, γ (°) | 90, 90, 90 |
| Matthews coefficient (Å3/Da) | 3.14 |
| Solvent content (%) | 60.9 |
| Data collection | |
| Wavelength (Å) | 1.00 |
| Resolution (Å) | 50–2.2 (2.28–2.2) |
| R sym (%)a | 3.3 (43.9) |
| No. of unique reflections | 68,373 |
| No. of reflections in R free set | 3,597 |
| Mean redundancy | 6.6 (3.6) |
| Overall completeness (%) | 96.7 (77.0) |
| Mean I/σ | 23.7 (4.1) |
| Refinement residuals | |
| Resolution (Å) | 50–2.2 (2.26–2.2) |
| R free (%)b | 23.0 (26.3) |
| R work (%)b | 19.4 (20.7) |
| Completeness (%) | 96.8 (75.3) |
| Model quality | |
| RMSD bond lengths (Å) | 0.008 |
| RMSD bond angles (°) | 1.1 |
| Molprobity Ramachandran distribution | |
| Most favored (%) | 98.6 |
| Allowed (%) | 1.4 |
| Disallowed (%) | 0.0 |
| Mean main chain B-factor (Å2) | 26.5 |
| Mean overall B-factor (Å2) | 31.7 |
| Mean ligand B-factor (Å2) | 32.3 |
| Mean solvent B-factor (Å2) | 31.2 |
| Model contents | |
| Protomers in ASU | 4 |
| Protein residues | 2–248 |
| Ligands | 4 AdoMet |
| No. of protein atoms | 8,092 |
| No. of ligand atoms | 108 |
| No. of water molecules | 537 |
| PDB accession code | 2YVL |
RMSD root-mean-square-deviation, ASU asymmetric unit
a R sym = Σhkl Σj|I j(hkl) − <I j(hkl)>|/ΣhklΣj I(hkl), where I j(hkl) and <I j(hkl)> are the intensity of measurement j and the mean intensity for the reflection with indices hkl, respectively
b R work, free = Σ|F obs − kF calc|/Σhkl F obs, where k is a scale factor, and the crystallographic R-factor is calculated including (R work) and excluding (R free) reflections. In each refinement, free reflections consist of 5 % of the total reflections