The objective of this project is to determine the 3-dimensional structure of the human beta2-adrenergic receptor, a G-protein coupled 7 transmembrane receptor, in the presence and absence of agonist and antagonist. Two approaches will be taken to determine the three- dimensional structure. The first approach is to determine the structure of the holo-receptor. The second approach is to truncate the receptor by removing the large soluble cytoplasmic regions of the receptor. The goal of working with the truncated molecule is to aid in the stabilization of the molecule and provide an alternative molecule for crystallization trials. The technique of electron diffraction of 2-dimensional crystals will be used. Because of the similarity in structure between bacteriorhodopsin and adrenergic receptor, the procedure used to determine the structure of bacteriorhodopsin will initially be followed.
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| Nogales, Eva (2018) Cytoskeleton in high resolution. Nat Rev Mol Cell Biol 19:142 |
| Downing, Kenneth H; Glaeser, Robert M (2018) Estimating the effect of finite depth of field in single-particle cryo-EM. Ultramicroscopy 184:94-99 |
| Nogales, Eva (2018) Cryo-EM. Curr Biol 28:R1127-R1128 |
| Sazzed, Salim; Song, Junha; Kovacs, Julio A et al. (2018) Tracing Actin Filament Bundles in Three-Dimensional Electron Tomography Density Maps of Hair Cell Stereocilia. Molecules 23: |
| Kamennaya, Nina A; Zemla, Marcin; Mahoney, Laura et al. (2018) High pCO2-induced exopolysaccharide-rich ballasted aggregates of planktonic cyanobacteria could explain Paleoproterozoic carbon burial. Nat Commun 9:2116 |
| Howes, Stuart C; Geyer, Elisabeth A; LaFrance, Benjamin et al. (2018) Structural and functional differences between porcine brain and budding yeast microtubules. Cell Cycle 17:278-287 |
| Glaeser, Robert M (2018) PROTEINS, INTERFACES, AND CRYO-EM GRIDS. Curr Opin Colloid Interface Sci 34:1-8 |
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| Han, Bong-Gyoon; Watson, Zoe; Cate, Jamie H D et al. (2017) Monolayer-crystal streptavidin support films provide an internal standard of cryo-EM image quality. J Struct Biol 200:307-313 |
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