. 1999 Jun 22;96(13):7149–7154. doi: 10.1073/pnas.96.13.7149

Table 1.

Statistics of crystallographic data and structure refinement

Protein	Ligand, 10 mM	Nucleobase density^*	Resolution, Å	Intensity data		R-factor	R-free
Protein	Ligand, 10 mM	Nucleobase density^*	Resolution, Å	R-sym, %	Completeness, %	R-factor	R-free
VP39	m³Ade	Complete	1.83	5.1	88.2	0.217	0.251
VP39	m¹Ade	Complete	2.2	5.5	77.7	0.206	0.256
VP39	Ade	None	1.92	8.2	90.7	0.236	0.251
VP39	m³Cyt	Complete	2.0	6.7	98.8	0.234	0.285
VP39	m¹Cyt	Complete	1.86	8.8	90.7	0.227	0.265
VP39	Cyt	None	1.86	6.7	90.2	0.218	0.261
Y22A	m⁷G	None	2.2	9.6	100	0.243	0.295
D182A	m⁷G	Complete	1.83	5.1	91.8	0.225	0.258
E233A	m⁷G	None	2.0	6.2	79.3	0.222	0.268
E233Q	m⁷G	Complete	2.2	4.7	89.7	0.211	0.255

Based on difference electron density contoured at either 2.5 or 2σ level (see also Materials and Methods, Figs. 1, 2, and 3, and ref. 6). For structures showing no density, lower contour levels yielded the same result.