Table 1.

EBOV NP oligomerization assessed by multi-angle light scattering.

#	Sample	VP35 1- 80 Added	Monomeric NP (kDa) Calculated	NP MALS
	Monomeric NP°-VP35 Co-expression
1	EBOV VP35 1-80 + NP 1-450		50	72
2	EBOV NP 1-450, AEX		50	>1000
	Monomeric NP°-VP35 fusions
3	EBOV VP35 1-80-NP 1-450		61	58
4	EBOV VP35 1-80-NP 1-739		94	110
5	SUDV VP35 1-49-NP 1-450		58	52
6	MARV VP35 1-41-NP 1-430		54	51
7	EBOV VP35 15-60-NP 34-367		42	40
	RNA-independent NP Oligomerization and Reversibility
8	EBOV VP35 1-80-TEV-NP 1-450		60	74
9	EBOV VP35 1-80 + NP 1-450, TEV cleaved		50	70
10	EBOV NP 1-450, TEV cleaved, AEX		50	>1000
11	EBOV NP 1-450	+	50	74
	Importance of Terminal Arm Domains in NP Oligomerization
12	EBOV NP 34-367		40	38
13	EBOV NP 34-367	+	40	51
14	MBP-EBOV NP 34-367		81	78
15	MBP-EBOV NP 34-367	+	81	85
16	MBP-EBOV NP 34-450		90	88
17	MBP-EBOV NP 1-367		85	>1000
18	MBP-EBOV NP 19-389		85	>1000
	Oligomeric NP-RNA
19	MBP-EBOV NP 1-450		94	>1000
20	MBP-EBOV NP 1-450	+	94	>1000
21	EBOV NP 1-450		50	>1000
22	EBOV NP 1-450	+	50	>1000
23	MBP-EBOV NP 1-739		127	>1000
24	MBP-EBOV NP 1-739	+	127	>1000

Calculated molecular weights are based on the expected mass of a single NP. Multi-angle light scattering data was collected with in-line size exclusion chromatography (SEC-MALS). In the Sample column hyphens between two protein domains represent protein fusions whereas plus signs indicate two distinct protein chains whether the result of co-expression or the result of a TEV protease cleavage. The data representing the co-expression of NP with VP35 (samples 1–2) or the RNA-independent NP oligomerization and reversibility of this oligomerization (samples 8–11) each represent a single protein preparation that was subsequently processed with additional steps such as cleavage by TEV protease, purification by anion exchange chromatography (AEX), or addition of purified VP35 1-80 peptide. See also Figure S1 for imaging of selected samples with negative stain electron microscopy.