Table 1.
Crystallographic statistics.
| Space group | C2221 |
| Unit cell lengths a, b, c (Å) | 117.22, 220.08, 56.31, |
| Resolution range (Å) | 40.0–2.7 (2.85–2.7)a |
| Wavelength (Å) | 0.972 |
| Number of measurements | 77501 (11497) |
| Number of unique reflections | 17725 (2631) |
| Multiplicity | 4.4 (4.4) |
| Completeness (%) | 88.4 (90.7) |
| Mean I/σI | 6.5 (2.8) |
| Wilson B (Å2) | 60.5 |
| Rmerge b | 0.134 (0.488) |
| Rwork c | 0.231 |
| Rfree d | 0.290 |
| RMSD bonds (Å) | 0.0054 |
| RMSD angles (°) | 0.871 |
| Ramachandran analysis (%) | |
| Favoured | 97.8 |
| Allowed | 2.0 |
| Outliers | 0.2 |
| Protein residues | 586 |
| Protein atoms total | 4398 |
| Overall B (Å2) subunit A, B | 38.9, 58.4 |
| Waters | 22 |
| Overall B (Å2) | 29.3 |
| Cl− | 1 |
| Overall B (Å2) | 47.2 |
a
Values in parentheses refer to the highest resolution bin of 2.85–2.7 Å.
b
Rmerge = ∑h∑i||(h,i) − 〈I(h)〉 ∑h∑i I(h,i).
c
Rwork = ∑h k l||Fo| − |Fc||/∑|Fo|, where Fo is the observed structure factor and Fc is the calculated structure factor.
d
Rfree is the same as Rwork except calculated using 5% of the data that are not included in any refinement calculations.