Apologies for the non-crystallographic question, but I would think the wide experience and vitality of this board might have some opinions on this topic.
We've sent out some samples for negative staining electron microscopy. They were stained with uranyl acetate on commercial grids and the resulting images seem to have a dispersity in the size of the little round blobs seen. Some of the blobs look like they might be what we see in our crystal structures. However, some of them are quite large. What have people's experience been with this technique and how close you get to an overall dimension for your protein or complex? How closely has that number been to results from other techniques (Xtallography, DLS, other hydrodynamic methods ....)? Is there some rule of thumb that describes if the image is slightly smaller or larger than the expected size? Thanks for your comments. Regards, Chad K. Park, Analyt. Biophys. Core Chem./Biochem., U. of AZ
