| Alternative title | Electron diffraction analysis of 2D protein crystals with large dhkl spacing |
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| DOI | Resolve DOI: https://doi.org/10.1017/S1431927610055923 |
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| Author | Search for: Li, Peng1; Search for: Malac, Marek1; Search for: Glaves, John Paul; Search for: Young, Howard1 |
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| Affiliation | - National Research Council Canada
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| Format | Text, Article |
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| Conference | Microscopy and Microanalysis 2010, Aug. 1–5, 2010, Portland, Oregon |
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| Abstract | Electron diffraction (ED) allows reliable identification of structure and orientation of crystalline samples. For biological/protein crystals with lattice (dₕₖₗ) from a few nm to a few tens nm the microscope camera length needs to be significantly increased. Thus, Fourier Transform (FT) of HRTEM images rather than ED have generally been used to retrieve structural information from such samples. Advantages of ED over HRTEM imaging include: 1) reduced irradiation dose; 2) ED can tolerate increased sample thickness; 3) the intensity of the ED spots is not affected by lens aberrations; 4) ED can tolerate sample drift [1]. Typical TEM lens settings are for camera length L = 10 to 300 cm, a good choice for a dₕₖₗ from 0.1 nm to 1 nm acquired at CCD camera or at the film plane. Here we show electron diffraction patterns from biological 2D crystals with large dₕₖₗ (lattice parameter a = 34 nm, b = 7.1 nm) in a JEOL 2200 FS TEM. Furthermore we show tomography results that demonstrate that the 2D crystals exhibit significant bending. |
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| Publication date | 2010-07-01 |
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| Publisher | Cambridge University Press |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | c92be193-2357-4187-adb7-096dafd421ee |
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| Record created | 2020-05-27 |
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| Record modified | 2020-05-27 |
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