Freeze-fracture electron microscopic analysis of solutions of biological molecules.
Freeze-fracture electron microscopy was used to study the morphology of proteins in solution. The size of the particles appearing on the fractured surface, replicated with tungstentantalum, were measured in a direction perpendicular to the shadowing angle. The distributions of the measured particle sizes could be correlated with the known shape and dimensions for each protein. It is concluded that freeze-fracture electron microscopy is a useful technique to study the morphology of biological molecules in solution, particularly hydrophobic proteins which may be difficult to study by other microscopic techniques.
D005614:Freeze Fracturing / Q000379:methods*; D006454:Hemoglobins; D006801:Humans; D008077:Lipoproteins, LDL; D008854:Microscopy, Electron / Q000379:methods*; D009211:Myoglobin; D011506:Proteins; D011130:RNA Ligase (ATP)
D006454:Hemoglobins; D008077:Lipoproteins, LDL; D009211:Myoglobin; D011506:Proteins; D011130:RNA Ligase (ATP)