Table 2. Comparison of indicators of map quality among various methods with RESOLVE .

		Initial phase map CC†		DM phase map CC†
Data set	Method	M.C.	S.C.	M.C.	S.C.	Mean phase error‡ 〈Δϕ〉DM (°)	Residues built with main chain§ (%)	Residues built with side chain§ (%)
Cytochrome c 3 (Fe-SAD)	Non-constraint	0.544	0.441	0.560	0.438	63.19	—	—
	Regular	0.544	0.441	0.584	0.440	62.43	—	—
	Direct	0.575	0.490	0.624	0.547	52.07	—	—
	ϕC selection¶	0.677	0.596	0.737	0.656	28.07
Lectin (Zn-SAD)	Non-constraint	0.617	0.339	0.589	0.332	72.02	40.8	8.8
	Regular	0.617	0.339	0.595	0.332	70.35	36.7	14.8
	Direct	0.717	0.470	0.836	0.613	54.28	84.3	80.8
	ϕC selection	0.840	0.592	0.901	0.692	32.72
Lysozyme (Gd-SAD)	Non-constraint	0.657	0.445	0.610	0.384	55.12	0.0	0.0
	Regular	0.657	0.445	0.662	0.422	52.82	0.0	0.0
	Direct	0.731	0.533	0.808	0.655	41.01	90.7	90.7
	ϕC selection	0.779	0.607	0.807	0.673	28.16
Lysozyme (S-SAD)	Non-constraint	0.618	0.425	0.437	0.344	62.31	10.4	8.5
	Regular	0.618	0.425	0.448	0.360	61.79	6.2	2.3
	Direct	0.698	0.492	0.774	0.620	44.67	93.8	93.8
	ϕC selection	0.775	0.568	0.821	0.671	29.26
Insulin (S-SAD)	Non-constraint	0.610	0.497	0.750	0.653	34.34	90.2	90.2
	Regular	0.610	0.497	0.762	0.679	33.02	91.2	91.2
	Direct	0.672	0.573	0.773	0.684	30.12	92.8	92.8
	ϕC selection	0.735	0.631	0.773	0.670	23.70
HptB (Se-SAD)	Non-constraint	0.590	0.406	0.611	0.428	55.54	58.6	12.6
	Regular	0.590	0.406	0.617	0.427	55.53	29.0	3.2
	Direct	0.641	0.538	0.781	0.622	38.14	87.6	85.1

^†Map CC, map correlation coefficient; M.C., main chain; S.C., side chain.

^‡Mean phase error 〈Δϕ〉_DM = , where ϕ(i) is the DM phase of the ith reflection and ϕ_c(i) is the model phase. N donates the total number of reflections.

^§The completeness of autobuilt residues with side chains was calculated with ARP/wARP. All proteins can be auto-built except for cytochrome c ₃_Fe, because the resolution limit of autobuilding in ARP/wARP is ∼2.5 Å.

^¶Phase ϕ₁ or ϕ₂ is selected based on the model phase ϕ_C.