Table 2.
Summary of x-ray crystallographic data collection and refinement statistics
| Crystal | AtPMT1·SAH·pCho | AtPMT2·SAH |
|---|---|---|
| Space group | P21 | P21 |
| Cell dimensions | a = 49.26 Å, b = 86.03 Å, c = 68.24 Å; β = 106.2° | a = 48.06 Å, b = 90.22 Å, c = 122.9 Å; β = 100.1° |
| Data collection | ||
| Wavelength (Å) | 0.979 | 0.979 |
| Resolution (Å) (highest shell) | 26.7–1.34 (1.36–1.34) | 30.0–1.50 (1.53–1.50) |
| Reflections (total/unique) | 238,716/121,932 | 742,803/162,824 |
| Completeness (highest shell) | 99.0% (99.4%) | 99.1% (99.6%) |
| 〈I/σ〉 (highest shell) | 30.2 (2.0) | 37.4 (2.1) |
| Rsym (highest shell) | 6.2 (53.9)% | 16.2 (60.6)% |
| Refinement | ||
| Rcryst/Rfree | 15.2/16.6% | 16.0/17.9% |
| No. of protein atoms | 4,022 | 7,543 |
| No. of water molecules | 650 | 1,175 |
| No. of ligand atoms | 74 | 104 |
| r.m.s.d., bond lengths (Å) | 0.006 | 0.006 |
| r.m.s.d., bond angles (°) | 1.106 | 1.071 |
| Average B-factor (Å2), protein, water, ligand | 21.3, 35.8, 14.3 | 29.1, 42.2, 22.2 |
| Stereochemistry: favored, allowed, outlier | 97.6, 2.4, 0.0% | 97.4, 2.4, 0.2% |