Table 2.

Data collection, phasing and refinement statistics for MAD (SeMet) structures

	Notch-Native 1	Jagged-Native 1	Jagged-Native 2	Jagged-SeMet 1		Jagged-SeMet 3
Data collection
Space group	P3121	C2	C2	C2		C2
Cell dimensions
a, b, c (Å)	28.0, 28.0, 281.7	61.0, 102.3, 62.7	60.6, 102.6, 61.2	61.2, 102.8, 60.7		61.0, 102.7, 59.9
α, β, γ (°)	90, 90, 120	90, 114.3, 90	90, 114.2, 90	90, 113.7, 90		90, 113.3, 90
				Peak 1	Peak 2	Remote	Peak
Wavelength	1.542	0.9340	0.9800	0.9788	0.9788	0.9537	0.9793
Resolution (Å)	24.3-2.6 (2.7-2.6)	57.1-2.5 (2.7-2.5)	55.8-3.1 (3.3-3.1)	56.0-2.8 (3.0-2.8)	51.4-2.7 (2.9-2.7)	51.6-2.9 (3.1-2.9)	51.4-3.1 (3.3-3.1)
R merge	6.2 (15.3)	9.2 (42.2)	10.3 (31.6)	13.5 (31.9)	11.6 (32.0)	11.6 (30.1)	12.5 (32.2)
I / σI	25.2 (5.3)	13.1 (3.3)	5.6 (2.3)	4.6 (2.1)	5.6 (2.1)	5.3 (2.1)	5.0 (2.0)
Completeness (%)	93.3 (93.3)	98.6 (98.6)	98.1 (98.1)	99.8 (99.2)	92.4 (92.8)	98.2 (98.6)	98.2 (98.7)
Redundancy (Ano)	8.2	3.7	3.4	(5.2)	(3.0)	(2.8)	(2.8)
Refinement
Resolution (Å)	24.3-2.6 (2.7-2.6)	48.5-2.5 (2.7-2.5)
No.	4080	11961
reflections
Rwork / Rfree	23.9 (29.1)/24.3 (36.3)	22.0 (26.3)/23.9 (30.8)
No. atoms
Protein	897	2229
Ligand/ion	8	9
Water	22	208
B-factors
Protein	34.3	32.3
Ligand/ion	33.9	36.4
Water	38.4	67.3
R.m.s deviations
Bond	0.005	0.007
lengths (Å)
Bond	0.68	0.72
angles (°)

^*Each dataset was collected using a single crystal.

^*Values in parentheses are for highest-resolution shell.