This program project represents a coordinated and mutually supporting effort to pursue research in structural biology in areas where electron diffraction and electron microscopy play a key, often unique role. Five of the projects within the Program represent applications of the methods of electron crystallography to specific problems in structural biology: these applications cover (A) structural intermediates in the ion-pumping cycle of bacteriorhodopsin, a model for membrane pumps which alternate between inward-facing and outward-facing protein conformation; (B) two-dimensional crystals of myelin basic protein, an essential component of the nerve- myelin crystallization studies of three members of a family of membrane receptors which include the beta-adrenergic conformational changes in tubulin, a target protein for the development of anti-cancer drugs, of which taxol is a prime example. Three additional projects seeks to further develop the instrumentation, experimental methodology and computational methodology used in high-resolution structural studies by electron crystallography. Project F1 will attempt to improve the quality of image data that an be captured with a CD camera; Project F2 will attempt to reduce the amount of specimen charging that occurs when recording high resolution images; and Project F3 will generate a set of molecular structure factors which more accurately account for modifications in the Coulomb shielding of the charge of the atomic nuclei that occurs when single atoms are covalently bonded into molecular structures. Two additional, already funded research projects which use equipment and facilities supported by this Program Project are also included as Associate Member projects. The Administrative Core (Project F) maintains and schedules major equipment, supports computer resources and provides a sense of intellectual community and common identity for all of the participants in the Program Project.
| Zhang, Rui; LaFrance, Benjamin; Nogales, Eva (2018) Separating the effects of nucleotide and EB binding on microtubule structure. Proc Natl Acad Sci U S A 115:E6191-E6200 |
| 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 |
| Kellogg, Elizabeth H; Hejab, Nisreen M A; Poepsel, Simon et al. (2018) Near-atomic model of microtubule-tau interactions. Science 360:1242-1246 |
| 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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