Analysis of Mitochondrial Membrane Protein Complexes by Electron Cryo-tomography

Author(s):  
Vicki A. M. Gold ◽  
Tobias Brandt ◽  
Laetitia Cavellini ◽  
Mickael M. Cohen ◽  
Raffaele Ieva ◽  
...  
2010 ◽  
Vol 31 (12) ◽  
pp. 1934-1936
Author(s):  
Steve T. Yeh ◽  
Mark G. Angelos ◽  
Yeong-Renn Chen

PROTEOMICS ◽  
2009 ◽  
Vol 9 (20) ◽  
pp. 4787-4798 ◽  
Author(s):  
Andreas O. Helbig ◽  
Marco J. L. de Groot ◽  
Renske A. van Gestel ◽  
Shabaz Mohammed ◽  
Erik A. F. de Hulster ◽  
...  

2004 ◽  
Vol 10 (S02) ◽  
pp. 1496-1497
Author(s):  
P A Bullough

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


1988 ◽  
Vol 21 (4) ◽  
pp. 429-477 ◽  
Author(s):  
W. Kühlbrandt

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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