Table 1.
Crystallographic data
| Protein | D128A | D128A/biotin |
|---|---|---|
| Space group | P21 | P21212 |
| Unit cell parameters | a = 48.0, b = 66.3, c = 82.3 Å; β = 97.3° | a = 55.7, b = 84.8, c = 50.0 Å |
| No. of tetramers per unit cell | 2 | 2 |
| Contents of the asymmetric unit | Tetramer | Dimer |
| Packing parameter VM, Å3/Da | 2.9 | 2.5 |
| Measured reflections, no. | 56,045 | 39,212 |
| Unique reflections, no. | 31,972 | 14,716 |
| Completeness | ||
| Overall, % | 85.0 | 88.0 |
| Outermost shell, % | 46.0 | 43.0 |
| Rmerge overall | 0.03 | 0.05 |
| Refinement | ||
| Nonhydrogen atoms, no. | 3,416 | 1,783 |
| Water molecules, no. | 178 | 104 |
| R factor* | 0.167 | 0.156 |
| Free R factor† | 0.243 | 0.243 |
| Average B factor,‡ Å2 | 32 | 31 |
| Ramachandran quality§ | 0.91 | 0.89 |
For all data with F > 4σ(F), R = Σhkl ∥Fo| − |Fc∥/Σhkl |Fo|.
For 10% of data with F > 4σ(F).
For all atoms.
Fraction (except Gly and Pro) in most favored regions (30).