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Computational Methods for High Resolution Analysis of Cryo-Electron Micrographs of Hepatitis B Virus Capsids

Published online by Cambridge University Press:  02 July 2020

J.F. Conway ,
N. Cheng ,
A. Zlotnick ,
P.T. Wingfield ,
S.J. Stahl  and
A.C. Steven
J.F. Conway
Affiliation:
Lab. of Structural Biology Research, National Institutes of Health, Bethesda, Maryland20892, USA.
N. Cheng
Affiliation:
Lab. of Structural Biology Research, National Institutes of Health, Bethesda, Maryland20892, USA.
A. Zlotnick
Affiliation:
Protein Expession Lab,National Institute of Arthritis, Musculoskeletal & Skin Diseases, National Institutes of Health, Bethesda, Maryland, 20892, USA.
P.T. Wingfield
Affiliation:
Protein Expession Lab,National Institute of Arthritis, Musculoskeletal & Skin Diseases, National Institutes of Health, Bethesda, Maryland, 20892, USA.
S.J. Stahl
Affiliation:
Protein Expession Lab,National Institute of Arthritis, Musculoskeletal & Skin Diseases, National Institutes of Health, Bethesda, Maryland, 20892, USA.
A.C. Steven
Affiliation:
Lab. of Structural Biology Research, National Institutes of Health, Bethesda, Maryland20892, USA.
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Extract

Cryo-electron microscopy allows high resolution structural studies of macromolecules or macro-molecular complexes. As structural analyses extend to higher resolutions, several major compu-tational problems arise in analyzing cryo-electron micrographs. One is the acute sensitivity of the sample to radiation damage, requiring that images be acquired at a low electron dose with conse-quently low signal-to-noise ratio (SNR), especially at higher spatial frequencies. Secondly, as the size of each digitized image grows, the duration of the computational procedures lengthen consider-ably. A third problem is the complex distortion imposed upon the images by the contrast transfer function (CTF) of the electron microscope. We have addressed these issues in the context of solving the Hepatitis B Virus (HBV) capsid structure, and have succeeded in improving the resolution of our model from 17À[4] to 9À[1] (Fig.l). This is sufficient to define part of the molecular structure, including a 4-helix bundle at the dimer interface which constitutes the protruding ‘spike’ domains seen on the surface of the capsid, as well as other helices elsewhere in the molecule.

Type
Computational Advances and Enabling Technologies for 3D Microscopies in Biology
Information
Microscopy and Microanalysis , Volume 3 , Issue S2: Proceedings: Microscopy & Microanalysis '97, Microscopy Society of America 55th Annual Meeting, Microbeam Analysis Society 31st Annual Meeting, Histochemical Society 48th Annual Meeting, Cleveland, Ohio, August 10-14, 1997 , August 1997 , pp. 1115 - 1116
Copyright
Copyright © Microscopy Society of America 1997

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References

1.Conway, J.F.,et al., Nature 386 (1997) 91.10.1038/386091a0CrossRefGoogle Scholar
2.Böttcher, B.et al., Nature 386 (1997) 88.10.1038/386088a0CrossRefGoogle Scholar
3.Trus, B.L.et al., Nature Struct. Biol. (1997) in press.Google Scholar
4.Zlotnick, A., et al., Biochemistry 35 (1996) 7412.10.1021/bi9604800CrossRefGoogle Scholar
5.Johnson, C.A.et al., Proc Super computing '94, Washington D.C. (1994) 550.10.1109/SUPERC.1994.344319CrossRefGoogle Scholar
6.Baker, T.S. and Cheng, R.H., J.Struct. Biol. 116 (1996) 120.10.1006/jsbi.1996.0020CrossRefGoogle Scholar