Structural analysis of membrane protein complexes by single particle electron microscopy

Methods ◽  
2007 ◽  
Vol 41 (4) ◽  
pp. 409-416 ◽  
Author(s):  
John L. Rubinstein
Keyword(s):  
Electron Microscopy ◽  
Structural Analysis ◽  
Membrane Protein ◽  
Single Particle ◽  
Protein Complexes ◽  
Membrane Protein Complexes ◽  
Single Particle Electron Microscopy

scholarly journals Structure and assembly of CAV1 8S complexes revealed by single particle electron microscopy

2020 ◽  
Vol 6 (49) ◽  
pp. eabc6185
Author(s):  
Bing Han ◽  
Jason C. Porta ◽  
Jessica L. Hanks ◽  
Yelena Peskova ◽  
Elad Binshtein ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Membrane Protein ◽  
Single Particle ◽  
Structural Organization ◽  
Building Blocks ◽  
Structural Features ◽  
Outer Ring ◽  
Current Evidence ◽  
Caveolin 1 ◽  
Single Particle Electron Microscopy

Highly stable oligomeric complexes of the monotopic membrane protein caveolin serve as fundamental building blocks of caveolae. Current evidence suggests these complexes are disc shaped, but the details of their structural organization and how they assemble are poorly understood. Here, we address these questions using single particle electron microscopy of negatively stained recombinant 8S complexes of human caveolin 1. We show that 8S complexes are toroidal structures ~15 nm in diameter that consist of an outer ring, an inner ring, and central protruding stalk. Moreover, we map the position of the N and C termini and determine their role in complex assembly, and visualize the 8S complexes in heterologous caveolae. Our findings provide critical insights into the structural features of 8S complexes and allow us to propose a model for how these highly stable membrane-embedded complexes are generated.

scholarly journals Preparation of Tunable Microchips to Visualize Native Protein Complexes for Single-Particle Electron Microscopy

2018 ◽  
pp. 45-58 ◽  
Author(s):  
Brian L. Gilmore ◽  
A. Cameron Varano ◽  
William Dearnaley ◽  
Yanping Liang ◽  
Bridget C. Marcinkowski ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Single Particle ◽  
Protein Complexes ◽  
Native Protein ◽  
Single Particle Electron Microscopy

scholarly journals Structure and assembly of CAV1 8S complexes revealed by single particle electron microscopy

2020 ◽  
Author(s):  
Bing Han ◽  
Jason C. Porta ◽  
Jessica L. Hanks ◽  
Yelena Peskova ◽  
Elad Binshtein ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Membrane Protein ◽  
Single Particle ◽  
Structural Organization ◽  
Building Blocks ◽  
Structural Features ◽  
Current Evidence ◽  
New Model ◽  
Caveolin 1 ◽  
Single Particle Electron Microscopy

AbstractHighly stable oligomeric complexes of the monotopic membrane protein caveolin serve as fundamental building blocks of caveolae. Current evidence suggests these complexes are disc shaped, but the details of their structural organization and how they assemble are poorly understood. Here, we address these questions using single particle electron microscopy of negatively stained recombinant 8S complexes of human Caveolin-1. We show that 8S complexes are toroidal structures ~15 nm in diameter that consist of an outer ring, an inner ring, and central protruding stalk. Moreover, we map the position of the N- and C-termini and determine their role in complex assembly, and visualize the 8S complexes in heterologous caveolae. Our findings provide critical insights into the structural features of 8S complexes and allow us to propose a new model for how these highly stable membrane-embedded complexes are generated.

Conformational Flexibility in Assembly of Photosynthetic Membrane Protein Complexes in vivo

2004 ◽  
Vol 10 (S02) ◽  
pp. 1496-1497
Author(s):  
P A Bullough
Keyword(s):  
Membrane Protein ◽  
Protein Complexes ◽  
Conformational Flexibility ◽  
Photosynthetic Membrane ◽  
Membrane Protein Complexes

Extended abstract of a paper presented at Microscopy and Microanalysis 2004 in Savannah, Georgia, USA, August 1–5, 2004.

Three-dimensional crystallization of membrane proteins

1988 ◽  
Vol 21 (4) ◽  
pp. 429-477 ◽  
Author(s):  
W. Kühlbrandt
Keyword(s):  
High Resolution ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Protein Complexes ◽  
Three Dimensional ◽  
Biological Macromolecules ◽  
X Ray ◽  
X Ray Crystallography ◽  
Membrane Protein Complexes ◽  
Essential Prerequisite

As recently as 10 years ago, the prospect of solving the structure of any membrane protein by X-ray crystallography seemed remote. Since then, the threedimensional (3-D) structures of two membrane protein complexes, the bacterial photosynthetic reaction centres of Rhodopseudomonas viridis (Deisenhofer et al. 1984, 1985) and of Rhodobacter sphaeroides (Allen et al. 1986, 1987 a, 6; Chang et al. 1986) have been determined at high resolution. This astonishing progress would not have been possible without the pioneering work of Michel and Garavito who first succeeded in growing 3-D crystals of the membrane proteins bacteriorhodopsin (Michel & Oesterhelt, 1980) and matrix porin (Garavito & Rosenbusch, 1980). X-ray crystallography is still the only routine method for determining the 3-D structures of biological macromolecules at high resolution and well-ordered 3-D crystals of sufficient size are the essential prerequisite.

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