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. 2006 Sep 8;362(1):78–88. doi: 10.1016/j.jmb.2006.06.079

Table 1.

Crystallographic data processing and refinement statistics

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
a

Rsym = ∑hkli|Ii(hkl−<I(hkl)>|/∑hkliIi(hkl), where <I> is the averaged intensity of the i observations of reflection hkl.

b

Outermost shell: the resolution range of the outermost shell is 2.77–2.67 Å.

c

Rcryst = ∑||Fo||Fc||/∑|Fo|, where Fo and Fc are observed and calculated structure factors, respectively.

d

Rfree is equal to Rcryst for a random subset of reflections (2.2%) not used in refinement.54