scholarly journals Functional and structural analysis of acetylcholine receptor-rich membranes after negative staining

FEBS Letters ◽  
1984 ◽  
Vol 173 (1) ◽  
pp. 217-221 ◽  
Author(s):  
Sigrid Reinhardt ◽  
Hardi Schmiady ◽  
Bernd Tesche ◽  
Ferdinand Hucho
Keyword(s):  
Structural Analysis ◽  
Acetylcholine Receptor ◽  
Negative Staining

Cloning and structural analysis of partial acetylcholine receptor subunit genes from the parasitic nematode Teladorsagia circumcincta

2001 ◽  
Vol 97 (4) ◽  
pp. 329-335 ◽  
Author(s):  
John Walker ◽  
Ruurdtje Hoekstra ◽  
Marleen H Roos ◽  
Lisa J Wiley ◽  
Anthony S Weiss ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Acetylcholine Receptor ◽  
Parasitic Nematode ◽  
Receptor Subunit ◽  
Teladorsagia Circumcincta

Structural analysis of the surface-layer protein of spirillum serpens by high-resolution electron microscopy

1983 ◽  
Vol 41 ◽  
pp. 738-739
Author(s):  
W. H. Wu ◽  
R. M. Glaeser
Keyword(s):  
Electron Microscopy ◽  
Surface Layer ◽  
Structural Analysis ◽  
High Resolution ◽  
Low Dose ◽  
High Resolution Electron Microscopy ◽  
Optical Diffraction ◽  
Surface Layer Protein ◽  
Morphological Unit ◽  
Resolution Electron

Spirillum serpens possesses a surface layer protein which exhibits a regular hexagonal packing of the morphological subunits. A morphological model of the structure of the protein has been proposed at a resolution of about 25 Å, in which the morphological unit might be described as having the appearance of a flared-out, hollow cylinder with six ÅspokesÅ at the flared end. In order to understand the detailed association of the macromolecules, it is necessary to do a high resolution structural analysis. Large, single layered arrays of the surface layer protein have been obtained for this purpose by means of extensive heating in high CaCl2, a procedure derived from that of Buckmire and Murray. Low dose, low temperature electron microscopy has been applied to the large arrays.As a first step, the samples were negatively stained with neutralized phosphotungstic acid, and the specimens were imaged at 40,000 magnification by use of a high resolution cold stage on a JE0L 100B. Low dose images were recorded with exposures of 7-9 electrons/Å2. The micrographs obtained (Fig. 1) were examined by use of optical diffraction (Fig. 2) to tell what areas were especially well ordered.

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