Table 2.
X-ray diffraction data collection and structure refinement statistics. Values in parentheses are for the highest-resolution shell
| Ligand-free ODH 6XUT |
ODH-GLC 6XUU |
ODH-G3G 6XUV |
|
|---|---|---|---|
| Data collection | |||
| Space group | P212121 | ||
| Unit-cell dimensions (Å) |
a = 48.87 b = 61.59 c = 195.09 |
||
| Resolution range (Å) |
97.55–1.43 (1.57–1.43) |
49.04–1.57 (1.67–1.57) |
97.33–1.75 (2.02–1.75) |
| Number of observations | 1,391,283 (295,026) | 1,064,709 (190,424) | 770,177 (268,996) |
| Unique reflections | 128,942 (25,836) | 103,996 (29,033) | 59,350 (20,470) |
| Completeness (%) | 99.9 (99.7) | 99.6 (98.8) | 99.9 (99.8) |
| Redundancy | 12.7 (11.4) | 6.6 (6.6) | 13.0 (13.1) |
| I/σ(I) | 14.5 (1.72) | 12.0 (1.36) | 7.0 (1.97) |
| Rmergea (%) | 7.1 (139.0) | 9.0 (141.0) | 17.5 (156.1) |
| CC1/2 | 100 (79.5) | 99.9 (55.8) | 99.9 (80.8) |
| Wilson B-value (Å2) | 22.0 | 28.6 | 25.9 |
| Refinement | |||
| Resolution range (Å) | 97.55–1.60 | 49.04–1.57 | 97.33–1.75 |
| Protein molecules per asymmetric unit | 1 | 1 | 1 |
| Rwork/Rfreeb | 0.165/0.196 | 0.162/0.189 | 0.168/0.207 |
| Deviations from ideal geometry | |||
| Bond (Å) | 0.0132 | 0.0127 | 0.0138 |
| Angles (Å) | 1.713 | 1.856 | 2.005 |
|
Ramachandran plot (%) Favored/allowed/outliers |
95.4/4.6/0 | 96.25/3.75/0 | 96.25/3.75/0 |
| Mean B-factors (Å2) | |||
| Protein | 42.2 | 36.9 | 48.7 |
| FAD/GLC/G3G | 33.4/-/- | 28.8/47.7/- | 40.1/-/61.7 |
| Water/sulfate | 41.8/55.9 | 42.7/85.9 | 52.6/105.3 |
| Number of atoms | |||
| Protein | 5023 | 4902 | 5059 |
| FAD/GLC/G3G | 53/-/- | 53/108/- | 53/-/115 |
| Water/sulfate | 466/40 | 363/20 | 303/15 |
a, where i runs over multiple observations of the same intensity, and j runs over all crystallographically unique intensities.
b, where |Fobs|> 0. Rfree is based on 5% of the data randomly selected and is not used in the refinement.