Table 2.
Data collection and refinement statisticsa
| GRNative | GRGSSG/NADP | GRGSH | GRNADPH | |
|---|---|---|---|---|
| Cell dimensions (Å) | ||||
| a | 120.4 | 119.4 | 120.0 | 119.7 |
| b | 62.4 | 62.2 | 62.3 | 62.6 |
| c | 84.0 | 83.9 | 84.0 | 84.2 |
| β (°) | 122.0 | 121.9 | 121.9 | 122.3 |
| Resolution limit (Å) | 0.95 | 1.1 | 1.0 | 1.0 |
| Unique observations | 290866 | 192429 | 232314 | 249970 |
| Multiplicity | 4.1 | 3.5 | 2.8 | 3.2 |
| Average I/σ | 11.3 (2.1) | 7.6 (1.9) | 7.1 (3.0) | 7.2 (2.0) |
| Rmeas (%) | 7.6 (45.2) | 8.1 (42.4) | 9.4 (29.4) | 9.8 (30.7) |
| Completeness (%) | 88 (45.2)b | 91 (74.8) | 84.1 (55.7)b | 90.9 (64.5)b |
| Refinement | ||||
| Reflections with F > 0 σ | 276635 | 147475 | 184585 | 194474 |
| Protein atoms | 3835 | 3849 | 3842 | 3842 |
| Heteroatoms | 78 | 208 | 178 | 131 |
| Solvent atoms | 825 | 916 | 906 | 858 |
| Hydrogen atoms | 3317.8 | 3359 | 3351.5 | 3359 |
| rmsd bonds (Å) | 0.018 | 0.015 | 0.016 | 0.016 |
| rmsd angles (Å) | 0.038 | 0.034 | 0.033 | 0.033 |
| <Bprotein> (Å2) | 14.2 | 20.4 | 17.4 | 17.8 |
| <Bligand> (Å2) | 9.0 | 20.1 | 13.8 | 12.1 |
| Rcryst (Rfree) (%) | 12.2 (15.1) | 11.4 (16.4) | 11.3 (14.7) | 12.33 (15.7) |
| Coordinate error (Å)c | 0.018 | 0.028 | 0.022 | 0.022 |
a
Numbers in parentheses refer to the highest-resolution shell.
b
The resolution cutoffs for which local completeness exceeds 75% are 0.97 Å, 1.05 Å and 1.1 Å for GRNative, GRGSH and GRNADPH, respectively.
c
Coordinate estimated standard uncertainty calculated using the Rfree variant of Cruickshank’s DPI24, with the equation σ(x, Bavg) = 1.0(Ni/nobs)1/2C−1/3Rfreedmin, where Ni is the number of non-hydrogen atoms, nobs is the number of unique observations, and C is the completeness.