. Author manuscript; available in PMC: 2010 Apr 7.

Published in final edited form as: J Struct Funct Genomics. 2008 Dec 20;10(2):127–136. doi: 10.1007/s10969-008-9054-7

Table 2.

Refinement statistics of Ufcl X-ray crystal structure

Maximum resolution (Å)	2.54
Number of observations	19,876 (4,903)
R_merge (%)^a	7.4 (19.8)
Number of reflections	19,876 (1,486)
Resolution range used in refinement	2.54 – 19.96
Completeness (%)	91.0 (76.9)
R factor (%)^b	23.3 (27.6)
free R factor (%)	27.9 (36.9)
rmsd in bond lengths (Å)	0.008
rmsd in bond angles (°)	1.2
Number of small molecules (per 4 protein protomers in asymmetric unit)	4 isothiocyanate ions 49 waters

$R_{m e r g e} = \sum_{h} \sum_{i} ∣ I_{h i} - 〈 I_{h} 〉 ∣ ∕ \sum_{h} \sum_{h i} I_{h i}$ . Numbers in parenthesis are for the highest resolution shell.

$R = \sum_{h} ∣ F_{h}^{o} - F_{h}^{c} ∣ ∕ \sum_{h} F_{h}^{o}$