Efficient expression, purification, and visualization by cryo-EM of unliganded near full-length HER3

Methods Enzymol. 2022:667:611-632. doi: 10.1016/bs.mie.2022.03.048. Epub 2022 Apr 5.

Abstract

Biochemical analyses of membrane receptor kinases have been limited by challenges in obtaining sufficient homogeneous receptor samples for downstream structural and biophysical characterization. Here, we report a suite of methods for the efficient expression, purification, and visualization by cryo-electron microscopy (cryo-EM) of near full-length Human Epidermal Growth Factor Receptor 3 (HER3), a receptor tyrosine pseudokinase, in the unliganded state. Through transient mammalian cell expression, a two-step purification with detergent exchange into lauryl maltose neopentyl glycol (LMNG), and freezing devoid of background detergent micelle, we obtained ~6Å reconstructions of the ~60kDa fully-glycosylated unliganded extracellular domain of HER3 from just 30mL of suspension culture. The reconstructions reveal previously unappreciated extracellular domain dynamics and glycosylation sites.

Keywords: Cryo-electron microscopy; HER receptors; Human epidermal growth factor receptors; Membrane proteins; Receptor tyrosine kinases.

MeSH terms

  • Animals
  • Cryoelectron Microscopy / methods
  • Detergents*
  • Humans
  • Mammals
  • Micelles*

Substances

  • Detergents
  • Micelles