Table 2.
Statistics of X-ray diffraction data and structure refinement.
| αMg+NADHγNADH | |
|---|---|
| Data collection | |
| Wavelength (Å) | 0.9785 |
| Space group | P3121 |
| a, b (Å) | 118.0 |
| c (Å) | 142.1 |
| Resolution (Å) | 50.0–2.40 (2.49–2.40)a |
| Observed reflections | 449,533 |
| Unique reflections (I/σ(I) > 0) | 45,428 |
| Average redundancy | 9.9 (8.9) |
| Average I/σ(I) | 22.6 (2.8) |
| Completeness (%) | 100.0 (100.0) |
| Rmerge (%)b | 12.1 (65.3) |
| Refinement and structure model | |
| No. of reflections (Fo > 0σ(Fo)) | 45,386 |
| Working set | 43,063 |
| Test set | 2,323 |
| R factor/Rfree factor (%)c | 21.1/23.6 |
| Total protein atoms | 5,048 |
| Total ligand atoms | 89 |
| Total solvent atoms | 94 |
| Wilson B factor (Å2) | 54.3 |
| Average B factor (Å2) | 64.5 |
| Protein | 63.9 |
| Mg (active site) | 52.6 |
| NADH (active/allosteric site) | 129.3/70.8 |
| Water | 54.3 |
| RMS deviations | |
| Bond lengths (Å) | 0.008 |
| Bond angles (°) | 1.3 |
| Ramachandran plot (%) | |
| Most favored | 96.5 |
| Allowed | 3.5 |
aNumbers in parentheses refer to the highest resolution shell.
bRmerge =
cR factor = ∑||Fo| − |Fc||/∑|Fo|.