Figure 1: Euglena IP39 protein was purified and reconstituted into lipid for the 2D crystal. | Nature Communications

Figure 1: Euglena IP39 protein was purified and reconstituted into lipid for the 2D crystal.

From: The four-transmembrane protein IP39 of Euglena forms strands by a trimeric unit repeat

Figure 1

(a) Purified IP39 was separated by SDS–PAGE and analysed by silver staining (left) or western blotting probed with anti-phosphotyrosine antibody (right). The apparent molecular weight of the major band (single arrowhead) is ~39 kDa, consistent with previous studies. The faint bands at the higher molecular weight (double arrowhead) correspond to dimers. (b) Size-exclusion chromatography of the purified IP39 protein shows a monodisperse peak. (c) A negatively stained image of the vesicular 2D crystal of IP39, observed by conventional electron microscopy. The black bar represents 400 nm. (Inset) Fourier transform of the negatively stained 2D crystal. The two independent lattices (a1* b1* and a2* b2*) indicate overlapping of the upper and lower side crystals in the vesicle.

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