Negative Staining Electron Microscopy of a Highly Flexible Sec1/Munc18 Protein Complex Stabilized by Glutaraldehyde Crosslinking.

Richard J Y Liu, Walter H A Kahr

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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

2 authors.

Richard J Y LiuDepartments of Paediatrics and Biochemistry, University of Toronto, Toronto, ON, Canada.

Walter H A KahrDepartment of Biochemistry, University of Toronto, Toronto, ON, Canada. walter.kahr@sickkids.ca.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Negative staining electron microscopy is one of the easiest ways to determine the shape and dimensions of multimeric protein complexes over 100 kDa molecular weight. This method requires small volumes (< 10 μL) of dilute protein (0.01-0.1 mg/mL). Here we describe a method for quickly crosslinking a protein sample and preparing negative stained grids, and we also describe how to label a biotinylated protein subunit with avidin to determine its position within a complex using negative staining EM. This method should be generally applicable for most soluble protein complexes.

Indexed as

Cross-Linking ReagentsGlutaralMicroscopy, ElectronMultiprotein ComplexesNegative StainingAvidinBiotinylationAvidinCross-Linking ReagentsGlutaralMultiprotein ComplexesAvidinCrosslinkingElectron microscopyNegative stainingProtein complexSec1/Munc18Structure determination

Identifiers

PMID39806158

DOI10.1016/j.jbc.2023.104718

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.