Table 2. I-SAD structure solution and refinement statistics.

	Protein
	NarQ		KR2		MACR		A2AAR-BRIL-ΔC
Structure solution and initial model building
Data	Eight anomalous + native	Data set #8 + native	Four anomalous + native		Three anomalous + native		Seven anomalous + native
Method	I-SAD	I-SIRAS	I-SAD	I-SIRAS	I-SAD	I-SIRAS	I-SAD	I-SIRAS
Initial resolution range (Å)	60−2.7	60−2.7	60−2.5	60−2.5	60−2.0	60−2.0	60−2.8	60−2.8
Number of residues in the protein	237		288		220		447
Substructure	14·I	10·I	16·I	17·I	26·I† 14·I	16·I	8·I	10·I
Resolution cutoff for substructure search (Å)	3.0	2.8	2.8	2.8	2.5	2.9	3.7	3.9
Resolution extension by native data (Å)	1.95	1.95	2.5	2.5	2.0	2.0	2.4	2.4
CCall/CCweak	40/15.4	31.8/18.1	42.6/20.7	37.7/25.1	28.8/15.3	29.8/19.6	35.0/14.8	36.7/21.4
Solvent content used in SHELXE (%)	47	47	58	59	50	50	49	49
CCmap, highest-resolution shell (%)	74	77	67	84	87	81	73	74
Number of Ala residues traced by SHELXE	178	187	212	208	190	272	155	250
Rwork/Rfree after initial model building (%)	23.0/28.5*	24.8/32.9*	22.4/30.1*	22.6/29.3*	24.2/29.2†‡ 29.4/32.7‡	29.7/46.2* 29.9/32.7‡	30.7/32.9‡	29.5/45.8*
Number of residues built in initial model building	215*	216*	235*	265*	343†‡ 300‡	69* 319‡	277‡	168*
Structure refinement
Data set (see Table 1)	8		3		3		2
Rwork/Rfree final (%)	19.0/26.2		19.0/22.6		17.7/21.9		23.4/29.4
Number in the ASU (asymmetric unit)
Protein residues	223		268		431		388
Water molecules	60		49		78		64
Iodide ions	12		20		22		6
Averaged B-factors (Å2)
Protein residues	43		40		38		38
Water molecules	34		44		47		27
Iodide ions	70		66		71		50
Ramachandran plot
Preferred	216 (99.1%)		259 (97.4%)		419 (98.4%)		373 (97.9%)
Allowed	2 (0.9%)		6 (2.2%)		7 (1.6%)		7 (1.8%)
Outliers	0		1 (0.4%)		0		1 (0.3%)

*Initial model built by ARP-wARP.

†Phasing carried out using phenix.autosol (all others used SHELXC/D/E).

‡Initial model built by phenix.autobuild.