High Resolution Imaging

Downing, Kenneth H.

Abstract

We will collect electron diffraction and image data used in the determination of the structure of so atomic resolution. High resolution images will be recorded unique combination of instrumentation including our resolution cold stage and spot-scan illumination system, that should give images of superior quality. For determining the three-dimensional structure, images will be recorded from specimens tilted up to 60 degrees, taking advantage of improvements we have made in overcoming problems of specimen flatness. Electron diffraction data will be recorded from specimens which have been labelled with heavy atom complexes at specific amino acids. Difference Fourier techniques will be used to determine the positions of these heavy atoms in the projection density map. This information will be useful in assigning regions of the three-dimensional density map to particular regions of the primary sequence.

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of General Medical Sciences (NIGMS)
• Type: Research Program Projects (P01)
• Project #: 5P01GM036884-05
• Application #: 3877922
• Support Year: 5
• Fiscal Year: 1990

Institution

• Name: Lawrence Berkeley National Laboratory
• DUNS #: 078576738
• City: Berkeley
• State: CA
• Country: United States
• Zip Code: 94720

Publications

Burkard, F; Chen, F; Kuziemko, G M et al. (1997) Electron density projection map of the botulinum neurotoxin 900-kilodalton complex by electron crystallography. J Struct Biol 120:78-84

Wolf, S G; Nogales, E; Kikkawa, M et al. (1996) Interpreting a medium-resolution model of tubulin: comparison of zinc-sheet and microtubule structure. J Mol Biol 262:485-501

Hud, N V; Downing, K H; Balhorn, R (1995) A constant radius of curvature model for the organization of DNA in toroidal condensates. Proc Natl Acad Sci U S A 92:3581-5

Perkins, G A; Downing, K H; Glaeser, R M (1995) Crystallographic extraction and averaging of data from small image areas. Ultramicroscopy 60:283-94

Nogales, E; Wolf, S G; Zhang, S X et al. (1995) Preservation of 2-D crystals of tubulin for electron crystallography. J Struct Biol 115:199-208

Han, B G; Wolf, S G; Vonck, J et al. (1994) Specimen flatness of glucose-embedded biological materials for electron crystallography is affected significantly by the choice of carbon evaporation stock. Ultramicroscopy 55:1-5

Han, B G; Vonck, J; Glaeser, R M (1994) The bacteriorhodopsin photocycle: direct structural study of two substrates of the M-intermediate. Biophys J 67:1179-86

Vonck, J; Han, B G; Burkard, F et al. (1994) Two progressive substrates of the M-intermediate can be identified in glucose-embedded, wild-type bacteriorhodopsin. Biophys J 67:1173-8

Wolf, S G; Mosser, G; Downing, K H (1993) Tubulin conformation in zinc-induced sheets and macrotubes. J Struct Biol 111:190-9

Perkins, G A; Burkard, F; Liu, E et al. (1993) Glucose alone does not completely hydrate bacteriorhodopsin in glucose-embedded purple membrane. J Microsc 169:61-5