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Immunoelectron Microscopy of Cryofixed Freeze-Substituted Yeast Saccharomyces cerevisiae
J. Fišerová, C. Richardson, MW. Goldberg,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- barvení a značení metody MeSH
- epoxidové pryskyřice chemie MeSH
- exprese genu MeSH
- fixace tkání metody MeSH
- fixativa chemie MeSH
- glutaraldehyd chemie MeSH
- imunoelektronová mikroskopie metody MeSH
- imunohistochemie metody MeSH
- komplex proteinů jaderného póru genetika metabolismus MeSH
- kryoprezervace metody MeSH
- mikrotomie MeSH
- mrazová substituce metody MeSH
- protilátky chemie MeSH
- Saccharomyces cerevisiae - proteiny genetika metabolismus MeSH
- Saccharomyces cerevisiae metabolismus ultrastruktura MeSH
- zalévání tkání metody MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Immunolabeling electron microscopy is a challenging technique with demands for perfect ultrastructural and antigen preservation. High-pressure freezing offers an excellent way to fix cellular structure. However, its use for immunolabeling has remained limited because of the low frequency of labeling due to loss of protein antigenicity or accessibility. Here we present a protocol for immunogold labeling of the yeast Saccharomyces cerevisiae that gives specific and multiple labeling while keeping the finest structural details. We use the protocol to reveal the organization of individual nuclear pore complex proteins and the position of transport factors in the yeast Saccharomyces cerevisiae in relation to actual transport events.
Citace poskytuje Crossref.org
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- $a Immunolabeling electron microscopy is a challenging technique with demands for perfect ultrastructural and antigen preservation. High-pressure freezing offers an excellent way to fix cellular structure. However, its use for immunolabeling has remained limited because of the low frequency of labeling due to loss of protein antigenicity or accessibility. Here we present a protocol for immunogold labeling of the yeast Saccharomyces cerevisiae that gives specific and multiple labeling while keeping the finest structural details. We use the protocol to reveal the organization of individual nuclear pore complex proteins and the position of transport factors in the yeast Saccharomyces cerevisiae in relation to actual transport events.
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- $a Richardson, Christine $u School of Biological and Biomedical Sciences, Durham University, South Road, Durham, DH1 3LE, UK.
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