Table 1.
Space group | Trigonal, P3221 |
---|---|
Unit cell dimensions (Å) | a = b = 138.48, c = 110.05 |
Resolution range (Å) | 24.67–2.67 |
Total reflections measured | 227,517 |
Unique reflections measured | 30,817 |
Rsym (%)a | 8.0 (35.8) |
I/σ(I) (outermost shell)b | 22.6 (4.7) |
Completeness (outermost shell) (%) | 91.8 (91.2) |
Rcryst (%)c | 22.3 |
Rfree (%)d | 25.9 |
A. Contents of the asymmetric unit | |
Protein atoms | 5798 |
Solvent molecules | 198 |
Ions | 12 (4 zinc and 8 calcium) |
B. r.m.s. deviation | |
Bond lengths (Å) | 0.007 |
Bond angles (°) | 1.35 |
C. Average B-factor (Å2) | |
All atoms (monomers A and B) | 44.7 (A); 49.9 (B) |
Main-chain atoms | 44.4 (A); 50.0 (B) |
Side-chain atoms | 45.0 (A); 49.8 (B) |
Ions (zinc and calcium) | 44.9 |
Solvent molecules | 34.1 |
Overall B-factor (Å2/Da) (from Wilson plot) | 63.1 |
Rsym = ∑hkl∑i|Ii(hkl−<I(hkl)>|/∑hkl∑iIi(hkl), where <I> is the averaged intensity of the i observations of reflection hkl.
Outermost shell: the resolution range of the outermost shell is 2.77–2.67 Å.
Rcryst = ∑||Fo|−|Fc||/∑|Fo|, where Fo and Fc are observed and calculated structure factors, respectively.
Rfree is equal to Rcryst for a random subset of reflections (2.2%) not used in refinement.54