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  Nuclear pore scaffold structure analyzed by super-resolution microscopy and particle averaging.

Szymborska, A., de Marco, A., Daigle, N., Cordes, V. C., Briggs, J. A. G., & Ellenberg, J. (2013). Nuclear pore scaffold structure analyzed by super-resolution microscopy and particle averaging. Science, 341(6146), 655-658. doi:10.1126/science.1240672.

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Szymborska, A., Author
de Marco, A., Author
Daigle, N., Author
Cordes, V. C.1, Author           
Briggs, J. A. G., Author
Ellenberg, J., Author
Affiliations:
1Research Group of Nuclear Architecture, MPI for biophysical chemistry, Max Planck Society, ou_578575              

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 Abstract: Much of life's essential molecular machinery consists of large protein assemblies that currently pose challenges for structure determination. A prominent example is the nuclear pore complex (NPC), for which the organization of its individual components remains unknown. By combining stochastic super-resolution microscopy, to directly resolve the ringlike structure of the NPC, with single particle averaging, to use information from thousands of pores, we determined the average positions of fluorescent molecular labels in the NPC with a precision well below 1 nanometer. Applying this approach systematically to the largest building block of the NPC, the Nup107-160 subcomplex, we assessed the structure of the NPC scaffold. Thus, light microscopy can be used to study the molecular organization of large protein complexes in situ in whole cells

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Language(s): eng - English
 Dates: 2013-07-112013-08-09
 Publication Status: Issued
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1126/science.1240672
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Title: Science
Source Genre: Journal
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Pages: - Volume / Issue: 341 (6146) Sequence Number: - Start / End Page: 655 - 658 Identifier: -