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. 2009 Mar 13;284(11):7339–7351. doi: 10.1074/jbc.M807398200

TABLE 2.

X-ray data collection and refinement statistics

Numbers in parentheses refer to the highest resolution shell.

Data collection
Space group C2221
Unit cell edges (Å) a = 138.6, b = 197.6, c = 83.0
X-ray source ESRF BM-14
Resolution range (Å) 30-2.5 (2.57-2.50)
No. of unique observations 37,806
Completeness (%) 95.4 (88.6)
Redundancy 4.9 (3.2)
Rmergea 0.064 (0.414)
<I/σI> 15.8 (2.7)
Refinement
No. of reflections work/test 35,893/1,911
No. of protein atoms 4,433
No. of ligand atoms 129
No. of waters 137
Average B-factors (Å2)
Protein monomers A/B/C 42.4/43.9/50.1
3′SL ligands/waters 66.7/43.5
Rcrystb 0.224
Rfree 0.263
Root mean square deviation bond distance (Å) 0.017
Root mean square deviation bond angle (°) 1.716
a

Rmerge = ∑hkli|Ihkl, i - 〈Ihkl〉|/∑hklIhkl〉.

b

Rcryst and Rfree = (∑||Fo| - |Fc||)/(∑|Fo|).