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. 2019 Jun 28;75(Pt 7):660–669. doi: 10.1107/S2059798319009094

Figure 2.

Figure 2

Cryo-EM and single-particle reconstruction of detergent-solubilized LAT1–CD98hc. (a) Micrograph of LAT1–CD98hc collected with the Volta phase plate after motion and CTF correction. The scale bar shown in the bottom left corner is 60 nm in length. The particles observed are consistent in size and shape with a heterodimeric, 123 kDa complex in DDM/CHS. (b) Representative 2D classes of the particles of LAT1–CD98hc used in 3D reconstruction; below, the resulting 3D map. The 2D classes and 3D map (mesh) are congruent and are characteristic of a HAT protein–detergent complex, with a small extracellular density and a large ellipsoidal detergent belt. LAT1 (magenta) and CD98hc (blue; PDB entry 6irs) are shown as ribbon models docked into the 3D map (EMD-4642). The particle box size was 200 Å with a mask diameter of 180 Å. (c) EM map density corresponding to the CD98hc ectodomain after multibody refinement with the crystal structure docked (PDB entry 2dh2). The A and C domains of CD98hc are coloured purple and red, respectively. (d) Fourier shell correlation (FSC) curves for the consensus reconstruction and for the ectodomain and micelle reconstructions. The resolution at a 0.143 FSC cutoff is ∼12 Å (consensus, blue), 11 Å (micelle, red) and 9 Å (ectodomain, green).