Table 1.
Crystallographic statistics
| A. Data collection | |||
| Space group | P6122 | ||
| Unit cell dimensions | |||
| a, b (Å) | 124.1 | ||
| c (Å) | 79.5 | ||
| Wavelength (Å) | 0.9792 (peak) | 0.9794 (inflection) | 0.9184 (remote) |
| f′, f″ (e) | − 8.09, 6.39 | − 9.87, 3.41 | − 4.1, 3.5 |
| Resolution (Å) (outer shell) | 25–2.4 (2.49–2.4) | 25–2.7 (2.8–2.7) | 25–2.9 (3.0–2.9) |
| Unique reflections | 14,593 (1422) | 10,250 (874) | 8440 (800) |
| Redundancya | 11.5 (10.5) | 6.6 (5.1) | 6.9 (7.2) |
| Completeness (%) | 99.9 (99.3) | 98.5 (87.1) | 99.8 (99.8) |
| <I/σ(I)> | 21.5 (3.8) | 21.7 (3.4) | 18.2 (3.9) |
| Rmergeb (%) | 9.0 (58.8) | 7.3 (42.9) | 10.2 (55.7) |
| B. Structure refinement | |||
| Resolution range (Å) | 25–2.4 | ||
| No. of reflections in refinement | 13,895 | ||
| R-factorc (%) | 22.3 | ||
| No. of reflections used for Rfree | 695 | ||
| Free R-factorc (%) | 27.6 | ||
| No. of protein atoms | 1476 | ||
| No. of water molecules | 114 | ||
| Wilson B-factor (Å2) | 45.3 | ||
| Average B-factor (Å2) | 51.9 | ||
| r.m.s. deviations | |||
| Bond lengthsd (Å) | 0.012 (0.02) | ||
| Bond anglesd (deg.) | 1.17 (2.0) | ||
| Ramachandran statistics | |||
| Most favoured regions (%) | 91.3 | ||
| Additionally allowed regions (%) | 8.7 | ||
| Generously allowed and disallowed regions (%) | 0 | ||
a
The average number of observations of the same reflection.
b
The value of the merging R factor between equivalent measurements of the same reflection, RI = ∑|I–<I>|/∑ I.
c
Crystallographic R-factor, R(free) = ∑||Fo|–|Fc||/∑|Fo|.
d
r.m.s. deviation from the standard values is given with target values in parentheses.