Fig. 4: Modelled RcpA-TadD complex with C14 symmetry.
From: Assembly mechanism of a Tad secretion system secretin-pilotin complex
a Cryo-EM 2D class averages of RcpAstrep-TadDFLAG complex exhibiting C14 symmetry. Samples were purified after heterologous expression in E. coli. Orientation bias yielded class averages between 0 and ~25Ëš tilt. b RcpA-TadDstrep complex purified directly from P. aeruginosa working with native expression levels. (Left) Western blot with anti-strep antibody confirmed the presence of TadDstrep in the eluate after purification by affinity chromatography. (Middle) Negative stain EM image of purified RcpA-TadDstrep complex. (Right) Class averages showing the presence of both C13 (73%) and C14 (27%) symmetries. The purification was repeated twice independently with similar particles obtained. c P. aeruginosa RcpA-TadDstrep C14 model. d Overlay of C14 symmetry model with typical C14 symmetry 2D class average.
