. Author manuscript; available in PMC: 2012 Sep 30.

Published in final edited form as: J Mol Biol. 2010 May 8;400(3):335–353. doi: 10.1016/j.jmb.2010.04.049

Table 3. Refinement statistics.

Proteins		Z2-bis	Z2-cac	Z2	Z3	Z6	Z8-PO₄	Z8-apo	Z16
Label		SeMet	SeMet	Native	Native	SeMet	Native	Native	SeMet
Resolution (Å)		1.70	1.75	2.00	3.00	2.30	1.76	2.60	2.70
Space Group		C222₁	C222₁	P2₁	P6₅	P3₁21	P2₁2₁2₁	P2₁2₁2	P4₃32
Unit cell	a (Å)	67.3	67.5	46.5	129.5	133.7	74.1	78.0	184.9
	b (Å)	88.5	87.7	98.4	129.5	133.7	79.4	115.0	184.9
	c (Å)	99.2	99.0	71.0	404.7	32.5	123.1	69.6	184.9
	β (°)			87.5
Z_a ^a		1	1	2	10	1	2	2	2
Solvent content		46%	45%	52%	59%	54%	53%	46%	72%
Unique		31298	28471	41368	72589	14044	68773	18510	28663
reflections
Total atoms		2306	2275	4643	21176	2229	5184	4317	3984
Protein atoms		2062	2066	4139	21117	2114	4552	4285	3849
Water		230	183	456	49	111	584	30	93
Ligand		bistris	SO₄	bistris		EDO	PO₄		MPD
Rwork ^b		18.1	18.9	17.8	23.2	18.1	18.2	25.3	20.5
Rfree ^c		21.1	23.4	24.6	27.7	24.5	22.2	32.4	25.6
RMS Bond (Å)		0.027	0.027	0.024	0.018	0.022	0.026	0.013	0.021
RMS angle (Å)		2.079	1.950	1.958	1.892	1.956	2.117	1.431	2.417
B_factor (Å²)		22.8	21.4	22.9	75.5	27.2	24.9	58.6	41.8
PDB code		3LI9	3LI8	3LIA	3LIB	3LIC	3LID	3LIE	3LIF

Za stands for number of molecules per asymmetric unit.

R_work = (Σ ∥Fo | − |Fc∥) / Σ|Fo|, where Fo and Fc denote observed and calculated structure factors, respectively.

R_free was calculated using 5% of data excluded from refinement.