. Author manuscript; available in PMC: 2010 Sep 1.

Published in final edited form as: Proteins. 2009 Sep;76(4):1049–1053. doi: 10.1002/prot.22469

TABLE I.

X-Ray Data Collection and Refinement Statistics

Space group	P6₃
% solvent	42
No. molecule in asymmetric unit	1
Data collection
Cell dimension: a, b, c (Å)	a= b=95.49 c= 56.96
Resolution range (Å)	20−2.0
No. observations	146433
No. unique reflections	19980
Completeness (%)^a	99.3(99.9)
R_merge ^b	0.069(0.306)
Refinement statistics
No. reflections	19952
No. residues	304
No. water molecules	267
R_cryst^c	0.197
R_free^d	0.255
RMS deviation
Bonds (Å)	0.017
Angles (°)	2.0

The values in parentheses are for the highest resolution shell

R_merge = Σ_hkl [(Σ_j | I_j - < I > | ) / Σ_j | I_j | ], for equivalent reflections

R_cryst = Σ_hkl | |F_o| - |F_c| | / Σ_hkl |F_o|, where F_o and F_c are the observed and calculated structure factors, respectively

R_free is computed for 5% of reflections that were randomly selected and omitted from the refinement