Table 1. Crystallographic data and refinement statistics.
|
Data collection* | |
| Unit Cell (Å) | a = 82.16, b = 82.16, c = 82.61 |
| Resolution range (Å) | 15-2.95 |
| Wavelength (Å) | 1.5418 |
| Observed reflections | 53485 |
| Unique reflections | 6274 |
| Completeness (%) | 99.0 (99.5) |
| Redundancy | 8.5 (8.8) |
| Rsyma | 0.122 (0.67) |
| I/SigI | 14.7 (3.3) |
| Space group | P41212 |
| Refinement | |
| Resolution range (Å) I > σ(I) | 15–2.95 |
| Rworkb | 0.22 |
| Rfreec | 0.27 |
| Root mean square deviation | |
| Bond lengths (Å) | 0.01 |
| Bond angles (°) | 1.599 |
| Average B-factors (Å2) | |
| Protein atoms (1514 atoms) | 58 |
| Ramachandran statistics | |
| Most favored and allowed regions (%) | 100 |
| Disallowed regions (%) | 0 |
Statistics from the current model.
aRsym = Σ|Ii–<I> |/Σ|Ii| where Ii is the intensity of the ith measurement, and <I> is the mean intensity for that reflection.
bRwork = Σ| Fobs–Fcalc|/Σ|Fobs| where Fcalc and Fobs are the calculated and observed structure factor amplitudes, respectively.
cRfree = as for Rwork, but for 10.0% of the total reflections chosen at random and omitted from refinement.
*Values in the parenthesis are the highest resolution bin values.