Fig. 1: Biochemical characterization and cryo-EM structure determination. | Nature Communications

Fig. 1: Biochemical characterization and cryo-EM structure determination.

From: Cryo-EM structure of the respiratory syncytial virus RNA polymerase

Fig. 1

a Schematic domain representation of the human respiratory syncytial virus (RSV) RNA polymerase (L:P complex), with labeled domain boundary (Alignment details in Supplementary Fig. 4). The domains with missing density are colored in gray. b The SDS-PAGE gel shows the quality of the wild-type (wt) and mutant RSV RNA polymerase, wt L:P, and L(D811A):P, respectively (repeated ≥ 5 times). c Elution profile of the purified L:P complex on the Superose 6 Increase 10/300 GL size-exclusion column (repeated ≥ 5 times). d The RNA dependent RNA polymerization assays show that the purified wt polymerase is active and can synthesis RNA with specific RNA templates (lane 6) compared with that of catalytically inactive polymerase L(D811A):P (lane 3). e Representative 2D class averages from the 200 kV cryo-EM dataset, selected amongst 125 classes. Scale bar: 100 Å. f The final cryo-EM density map with the model (colored as a) in two orientations.

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