. Author manuscript; available in PMC: 2007 Oct 15.

Published in final edited form as: J Struct Biol. 2006 Dec 24;158(3):494–502. doi: 10.1016/j.jsb.2006.12.004

Table II.

Crystallographic refinement statistics

Space group	R32
Cell dimensions	a=146.30 Å, b=146.30 Å,c=514.30 Å, α=β=90°, γ=120°
Volume fraction of protein	73%
V_m (Å³/Dalton)	4.53
Total number residues	1019 /asu
Overall temperature factor	69.7 Å²
Resolution range of reflections used	50.0–3.1 Å
R factor ^a	0.305 (0.420)
Free R factor^a	0.341 (0.476)
Reflections in working set^a	36947 (6113)
Reflections in test set^a	1952 (289)
Total data completeness (working set + test set)^a	38899/99.6 % (6402/100%)
R.M.S. deviations: bond	0.009
angle	1.6

Numbers in parentheses are related to the highest resolution shell (3.29–3.10 Å)