Author:
Löschberger Anna,Franke Christian,Krohne Georg,van de Linde Sebastian,Sauer Markus
Abstract
We combine super-resolution fluorescence localization microscopy with scanning electron microscopy to map the position of proteins of nuclear pore complexes in isolated Xenopus laevis oocyte nuclear envelopes with molecular resolution in both imaging modes. We use the periodic molecular structure of the nuclear pore complex to superimpose direct stochastic optical reconstruction microscopy images with a precision of < 20 nm on electron micrographs. The correlative images demonstrate quantitative molecular labeling and localization of nuclear pore complex proteins by standard immunocytochemistry with primary and secondary antibodies and reveal that the nuclear pore complex is composed of eight gp210 protein homodimers. In addition, we find subpopulations of nuclear pore complexes with ninefold symmetry that are found occasionally among the more typical eightfold symmetrical structures.
Publisher
The Company of Biologists
Cited by
105 articles.
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