Fig. 1: Extreme membrane curvature facilitates full-length E-Syt1-dependent lipid transfer.
From: Insights into membrane association of the SMP domain of extended synaptotagmin

a, Schematic representation of full-length E-Syt1-dependent lipid transfer and liposome tethering in the presence of Ca2+. b, Time courses of lipid transfer between distinctly sized ER-like donor proteoliposomes containing E-Syt1 and PM-like acceptor liposomes in the presence of Ca2+ at room temperature as assessed by dequenching of NBD-PE fluorescence (mean ± SD, n = 3 independent experiments). c, Negative-staining TEM images showing E-Syt1-containing ER-like donor proteoliposomes prepared from sonication and extrusion through filters with 30 nm pores. Scale bar, 100 nm. d, Size distribution of proteoliposomes measured from negative-staining TEM images in (c). Average diameters are presented as mean ± SD (n = 286 and 203 proteoliposomes from left to right). e, Schematic of assembled DNA bricks and steps for DNA brick-assisted liposome sorting. f, Negative-staining TEM images showing distinctly sized E-Syt1-containing ER-like donor proteoliposomes prepared from extrusion through filters with 30 nm pores followed by DNA-brick-assisted sorting. Scale bar, 100 nm. g, Size distribution of proteoliposomes measured from negative-staining TEM images in F. The histograms are fitted by Gaussian functions. Average diameters are presented as mean ± SD (n = 152, 306, 361 and 1165 proteoliposomes from left to right). Source data are provided as a Source Data file.