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Researchers have used quick-freeze/deep-etch electron microscopy of recombinant proteins adsorbed to mica to investigate the oligomeric ATPase NSF. It was found that NSF, whose hydrolytic activity is vital for membrane fusion, is a hollow 10 nm x 16 nm cylinder. Its conformation is determined by nucleotide binding. It was possible to show that conformational changes take place in NSF during its ATPase cycle. Researchers also assessed the structure and geometry of the SNAP receptors which are dissociated by NSF.

The Golgi cisternal structure and the morphological transitions caused by different internal incubations, visualized and analyzed by high resolution 3-O electron microscopy, reveal two distinct surface coatings with a variety of distribution and apparent functions. One of the coatings, the coatomer coat, is tightly packed with 10-nanometer-sized surface particles, which are found only in regions of membrane formation. The second coating is finer and is distributed in the periphery of the cisternal. This layer stabilizes the membrane curvature related to the edges and tubules.