Skip to main content
. Author manuscript; available in PMC: 2020 May 11.
Published in final edited form as: Cell Rep. 2020 Jan 7;30(1):153–163.e5. doi: 10.1016/j.celrep.2019.12.020

Figure 1. The SFTSV L Endonuclease Domain Is a Monomer in Solution and Adopts a Mixed Alpha-Beta Fold.

Figure 1.

(A) SEC-MALS analysis of SFTSV L 1–231 aa. The determined mass of SFTSV L 1–231 aa (green) is 2.71 ± 0.01 × 104 Da. The theoretical mass for the monomer is 2.76 × 104 Da. Independent experiments were carried out in triplicate and representative data are shown here. Inset: Coomassie-stained SDS-PAGE of purified, recombinant N-terminal His-tagged SFTSV L endonuclease domain 1–231 aa (arrowhead).

(B) X-ray crystal structure of the SFTSV L endonuclease domain. Secondary structural elements that form the α helices, the β sheets, and the loop regions are annotated based on the relative position from the N terminus.