Table 1.
Data collection and structure refinement statistics
| Data collection | |
|---|---|
| Space group | P212121 |
| Unit cell dimensions, (Å) | a = 135.1, b=180.6, c = 187.5 |
| Wavelength (Å) | 0.976 |
| Resolution, Å (outer shell) | 25–3.0(3.11–3.0) |
| Unique reflections | 86,130(6572) |
| Redundancya | 4.8(3.5) |
| Completeness (%) | 94.0(72.6) |
| <I/σ(I)> | 13.5(2.0) |
| Wilson B-factor (Å2) | 67 |
| Rmergeb (%) | 10.8(51.3) |
| Structure refinement | |
| Resolution range (Å) | 3.0–25 |
| Number of reflections in refinement | 85,189 |
| R-factorc (%) | 21.3 |
| Number of reflections used for Rfree | 853 |
| Free R-factorc (%) | 27.2 |
| Number of protein atoms | 26,332 |
| Number of water molecules | 38 |
| Average B-factor (Å2) | 77 |
| R.m.s.d. | |
| Bond lengthsd (Å) | 0.01 (0.02) |
| Bond anglesd (degree) | 1.2 (2.0) |
| Ramachandran statistics | |
| Most favored regions (%) | 90.5 |
| Allowed regions (%) | 9.5 |
| Disallowed regions(%) | 0 |
aThe average number of observations of the same reflection.
bThe value of the merging R factor between equivalent measurements of the same reflection, RI = ∑ |I − <I>| / ∑ I.
cCrystallographic R-factor, R(free) = ∑ ||Fo| − |Fc|| / ∑ |Fo|.
dR.m.s.d. from the standard values are given with target values in parentheses.