Table 1.
Crystallographic parameters, data collection and refinement statistics.
| H53D+FAD | H53D+FAD+dUMP | |
|---|---|---|
|
| ||
| Crystallographic parameters | ||
| Space group | P212121 | P212121 |
| Unit-cell dimensions (Å) | 53.99, 116.64, 141.38Å 90.0, 90.0, 90.0° |
54.37, 116.67, 141.42Å 90.0, 90.0, 90.0° |
|
| ||
| Data collection statistics | ||
| Resolution limits (Å) | 38.2-2.03 | 38.3-1.85 |
| No. of observed reflections | 354413 | 278376 |
| No. of unique reflections | 58450 | 72637 |
| Completeness overall/outer shell |
99.8/99.2 | 93.4/62.9 |
| Rsyma (%) overall/outer shell |
7.1/97.1 | 3.3/56.8 |
| I/σ Overall/outer shell |
20.1/1.9 | 28.6/1.97 |
|
| ||
| Refinement statistics | ||
| Resolution limits | 38.2-2.05 | 38.3-1.85 |
| Number of reflections/% | 55525/99.8 | 69005/93.4 |
| Reflections used for Rfree | ||
| Rfactorb (%) | 19.6 | 17.0 |
| Rfree (%) | 24.9 | 21.1 |
| Model contents/average B(Å2) | ||
| Protein atoms | 7221/44.3 | 7417/31.5 |
| Ligand atoms | 140/77.3 | 181/52.0 |
| Ions/buffer atoms | 13/69.1 | 14/61.5 |
| Water molecules | 150/46.3 | 305/38.2 |
| RMS deviations | ||
| Bond length (Å) | 0.014 | 0.015 |
| Bond angle (°) | 1.571 | 1.756 |
a
Rsym=Σ | Iavg-Ii|/Σ Ii
b
Rfactor=Σ|Fp-Fpcalc |/ΣFp, where Fp and Fpcalc are observed and calculated structure factors; Rfree is calculated with 5% of the data.