Table 2.

Crystallographic and phasing statistics for iodide SAD phased SSGCID structures

PDB ID	Phasing resolution (Å)	Space group	Multiplicitya	SigAnob	Residues in AU	Solvent content (%)	Iodide sitesc	FOMd	Method
3K9G	2.25	P43212	12.5	1.43	1 × 267	51	2/12	0.45	SAD
3KM3	2.1	H3	5.6	1.16	2 × 206	42	13/16	0.24	SAD
3KW3	2.95	C2	3.8	1.26	2 × 372	45	4/0	0.29	SAD/MR
3LA9	2.05	H3	5.4	2.08	1 × 178	29e	4/9	0.49	SAD
3LR0	1.9	P3221	11.2	2.33	1 × 123	46	6/6	0.44	SAD
3LR5	2.3	P212121	3.6	0.99	2 × 123	43	4/5	0.39	SAD
3LUZ	2.05	P21	3.8	1.22	2 × 267	37	6/13	0.50	SAD/MR
3MD7	2.00	C2221	6.5	1.34	2 × 272	40	11/0	0.49	SAD
3MEN	1.9	P212121	6.8	1.24	4 × 341	43	24/35	0.41	SAD
3NJB	2.2	I23	10.9	1.27	2 × 333	59	9/50	0.39	SAD
3O2E	1.95	P41212	10.3	1.70	1 × 90	25	5/9	0.53	SAD
3OIB	2.1	C2	3.7	1.78	2 × 403	48	15/50	0.55	SAD
3OL3	1.95	P212121	6.6	1.91	2 × 103	51	9/21	0.43	SAD
3P96	2.75	I222	7.7	1.70	1 × 418	53	15/0	0.41	SAD
3PFD	2.1	P21	3.7	1.19	4 × 389	48	8/109	0.53	SAD/MR
3PM6	2.5	P21	3.8	1.64	2 × 302	46	5/31	0.46	SAD/MR

^aOverall multiplicity for anomalous scaled data; multiplicity for merged data is ca. twofold higher

^bSigAno is the mean anomalous difference in units of its estimated standard deviation (|F ⁺ − F ⁻|/σ) [24]

^cThe number of iodide sites input into Phaser EP [27], followed by the number of iodide sites in the final model. For 3KW3, 3MD7 and 3P96 only the high-resolution native data was deposited into the PDB, and thus the final model contained no iodide ion sites

^dOverall Figure of Merit (FOM) from Phaser EP [27] prior to density modification

^eThe solvent content was calculated based on the full length tagged protein. This protein only crystallized using in situ proteolysis with chymotrypsin [22], and thus, the true solvent content is likely higher [7]