Erratum to: The Use of Freeze-Fracture and Freeze-Etching Electron Microscopy for Phase Analysis and Structure Determination of Lipid Systems

1984 ◽  
pp. 726-726
Author(s):  
K. L. Mittal ◽  
B. Lindman
Keyword(s):  
Electron Microscopy ◽  
Phase Analysis ◽  
Structure Determination ◽  
Freeze Fracture ◽  
Freeze Etching

Freeze-Fracture Replication of Frozen Outer Segments of Rat Retinal Rods

1969 ◽  
Vol 27 ◽  
pp. 392-393
Author(s):  
Thomas S. Leeson ◽  
C. Roland Leeson
Keyword(s):  
Electron Microscopy ◽  
Cross Section ◽  
Outer Segment ◽  
Freeze Fracture ◽  
X Ray Diffraction ◽  
X Ray ◽  
Outer Segments ◽  
Retinal Rods ◽  
Temperature Electron ◽  
Freeze Etching

Numerous previous studies of outer segments of retinal receptors have demonstrated a complex internal structure of a series of transversely orientated membranous lamellae, discs, or saccules. In cones, these lamellae probably are invaginations of the covering plasma membrane. In rods, however, they appear to be isolated and separate discs although some authors report interconnections and some continuities with the surface near the base of the outer segment, i.e. toward the inner segment. In some species, variations have been reported, such as longitudinally orientated lamellae and lamellar whorls. In cross section, the discs or saccules show one or more incisures. The saccules probably contain photolabile pigment, with resulting potentials after dipole formation during bleaching of pigment. Continuity between the lamina of rod saccules and extracellular space may be necessary for the detection of dipoles, although such continuity usually is not found by electron microscopy. Particles on the membranes have been found by low angle X-ray diffraction, by low temperature electron microscopy and by freeze-etching techniques.

Low-resolution structure determination of Na+-translocating NADH:ubiquinone oxidoreductase fromVibrio choleraebyab initiophasing and electron microscopy

2012 ◽  
Vol 68 (6) ◽  
pp. 724-731 ◽  
Author(s):  
Vladimir Y. Lunin ◽  
Natalia L. Lunina ◽  
Marco S. Casutt ◽  
Kèvin Knoops ◽  
Christiane Schaffitzel ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Structure Determination ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Low Resolution ◽  
Resolution Structure

scholarly journals The crystal lattice of Paramecium trichocysts before and after exocytosis by X-ray diffraction and freeze-fracture electron microscopy.

1987 ◽  
Vol 105 (4) ◽  
pp. 1649-1662 ◽  
Author(s):  
L Sperling ◽  
A Tardieu ◽  
T Gulik-Krzywicki
Keyword(s):  
Electron Microscopy ◽  
Freeze Fracture ◽  
X Ray ◽  
Before And After ◽  
Ordered Array ◽  
Extracellular Form ◽  
Freeze Etching ◽  
Freeze Fracture Electron Microscopy ◽  
Genetically Determined ◽  
Fracture Electron

Paramecium trichocysts are unusual secretory organelles in that: (a) their crystalline contents are built up from a family of low molecular mass acidic proteins; (b) they have a precise, genetically determined shape; and (c) the crystalline trichocyst contents expand rapidly upon exocytosis to give a second, extracellular form which is also an ordered array. We report here the first step of our study of trichocyst structure. We have used a combination of x-ray powder diffraction, freeze-etching, and freeze-fracture electron microscopy of isolated, untreated trichocysts, and density measurements to show that trichocyst contents are indeed protein crystals and to determine the elementary unit cell of both the compact intracellular and the extended extracellular form.

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