Table 1. Crystallographic data and refinement statistics.
Data collection | |
Wavelength (Å) | 0.97 |
Space group | P 63 2 2 |
Unit cell dimensions (Å) | a=b=135.72c=202.13 |
Molecules/asymmetric unit | 4 |
Resolution range (Å) | 50.00–2.8 |
Unique observations | 27,721 |
Completeness (%)* | 99.8 (100) |
Rsym (%) | 7.2 (7.3) |
I/s(I) | 11.2 (1.9) |
Refinement | |
Resolution (Å) | 10–2.8 |
Rcryst, Rfree * | 0.22 (0.39), 0.26 (0.36) |
Reflections (working/test) | 25,543/1,346 |
Protein atoms | 3,720 |
Sulfate atoms | 30 |
R.m.s.d. bond lengths (Å) | 0.01 |
R.m.s.d. angles (Å2) | 1.5 |
<B> protein (Å2) : | 75 |
Ramachandran plot | |
Most favoured (%)† | 90.7 |
Allowed (%) | 7.8 |
Generously allowed (%) | 1.5 |
R.m.s.d., root mean-squared deviation.
*High-resolution shell for data collection is 2.8–2.85 and for refinement 2.8–2.87.
†Calculated by PROCHECK.