Sattin, B. D., and M. C. Goh. 1999. RecA fibril assembly and structure in near physiological conditions by atomic force microscopy. Biophysical Journal. 76:A323-A323.

Paige, M. F., J. K. Rainey, and M. C. Goh. 1998. Fibrous long spacing collagen ultrastructure elucidated by atomic force microscopy. Biophysical Journal. 74:3211-3216.

Description:

Some areas of research push the limits of the AFM (Atomic Force Microscope) by examining its application towards biological systems. One system under study is the bacterial RecA protein. This protein is involved in controlling the evolution of bacterial species. It is intimately involved in the SOS mutagenesis pathway (which forcefully incorporates mutations into a bacterial genome) and homologous recombination.

This gives us the potential to image biological systems, under physiological conditions, at a resolution comparable to electron micrscopy.  Electron microscopy experiments are done with the RecA all dried out.  Thus we decided to look at them in physiological salt and pH buffer conditions.  These fibrils are 12 nm in diameter. The above image is a 1 micron scan, a topographic image of RecA protein in buffer, pH=7 taken on a DI Nanoscope III with TappingMode® under fluid.


 

Please contact the webmaster if you would like to submit an image