TABLE 1.
Data collection and refinement statistics
One crystal was used for this structure. Values in parentheses are for the highest resolution shell.
| Data collection | |
| Source | SSRF BL17U |
| Wavelength (Å) | 0.99582 |
| Space group | H3 |
| cell dimensions | |
| a, b, c (Å) | 114.60, 114.60, 62.11 |
| α, β, γ (°) | 90.00, 90.00, 120.00 |
| Resolution (Å) | 50–1.68 (1.74–1.68) |
| Mosaicity | 0.19–0.46 |
| Rmergea (%) | 5.5 (26.8) |
| I/σI | 32.9 (8.2) |
| Completeness (%) | 99.2 (93.6) |
| Redundancy | 5.5 (5.6) |
| Refinement | |
| Resolution (Å) | 33–1.68 |
| No. of reflections | 34,430 |
| Rwork/Rfreeb (%) | 17.04/18.72 |
| No. of atoms | 2414 |
| Protein | 2131 |
| Ligand/ion | 15 |
| Water | 268 |
| B-factors | 23.52 |
| Protein | 22.68 |
| Ligand/ion | 13.83 |
| Water | 30.70 |
| r.m.s. deviations | |
| Bond lengths (Å) | 0.008 |
| Bond angles (°) | 1.197 |
| Ramachandran plot statisticsc (%) | |
| Most favored | 91.1 |
| Additional allowed | 8.9 |
| Generously allowed | 0.0 |
| Disallowed | 0.0 |
a Rmerge = ΣhΣi|Ih,i − Ih|/ΣhΣiIh,i, where Ih is the mean intensity of the i observations of symmetry related reflections of h.
b R = Σ|Fobs − Fcalc|/ΣFobs, where Fcalc is the calculated protein structure factor from the atomic model (Rfree was calculated with 5% of the reflections selected randomly).
c Ramachandran plot was performed by Procheck.