Super-resolution imaging visualizes the eightfold symmetry of gp210 proteins around the nuclear pore complex and resolves the central channel with nanometer resolution

Super-resolution imaging visualizes the eightfold symmetry of gp210 proteins around the nuclear pore complex and resolves the central channel with nanometer resolution

Löschberger, A.
Van de Linde, S.
Debauvalle, M.C.
Rieger, B.
Heilemann, M.
Krohne, G.
Sauer, M.

Applied Sciences

IST/Imaging Science and Technology

2012-02-01

One of the most complex molecular machines of cells is the nuclear pore complex (NPC), which controls all trafficking of molecules in and out of the nucleus. Because of their importance for cellular processes such as gene expression and cytoskeleton organization, the structure of NPCs has been studied extensively during the last few decades, mainly by electron microscopy. We have used super-resolution imaging by direct stochastic optical reconstruction microscopy (dSTORM) to investigate the structure of NPCs in isolated Xenopus laevis oocyte nuclear envelopes, with a lateral resolution of ~15 nm. By generating accumulated super-resolved images of hundreds of NPCs we determined the diameter of the central NPC channel to be 41±7 nm and demonstrate that the integral membrane protein gp210 is distributed in an eightfold radial symmetry. Two-color dSTORM experiments emphasize the highly symmetric NPCs as ideal model structures to control the quality of corrections to chromatic aberration and to test the capability and reliability of super-resolution imaging methods.

super-resolution imaging
nuclear pore complex
dSTORM
single-molecule localization
OA-Fund TU Delft

http://resolver.tudelft.nl/uuid:7372fcd4-d620-44f0-95a9-b54eefdc7984

doi:10.1242/​jcs.098822

Company of Biologists

0021-9533

Journal of Cell Science, 125, 2012

Institutional Repository

journal article

© 2012 Creative Commons Attribution Non-Commercial Share Alike License