Biology Reference
In-Depth Information
Chapter 2
HIGHRESOLUTION ATOMIC FORCE
MICROSCOPY OF NATIVE MEMBRANES
Nikolay Buzhynskyy, Lu-Ning Liu, Ignacio Casuso and
Simon Scheuring
Institut Curie, U1006 INSERM, 26 rue d'Ulm, Paris, France
Simon.Scheuring@curie.fr
2.1 AFM IN STRUCTURAL BIOLOGY OF MEMBRANE PROTEINS
The atomic force microscope (AFM) has developed into a powerful tool in
membrane protein research. 1 Two reasons why AFM is the tool of choice
for membrane protein studies are its capability to study single molecules
in a sample that needs relatively little prior biochemical treatment and the
nativeness of the sample studied.
All techniques, with the exception of AFM, appeal to molecule
averaging to obtain structural information ( Fig. 2.1 ) . Depending on the
signal-to-noise ratio (SNR) provided by a technique, a certain numbers
of molecules must be merged to acquire structural information. The
averaging methodology varies among techniques and can imply Fourier
transformations for techniques where proteins are crystallized (X-ray
and electron crystallography), computational overlay of images where
individual molecules are imaged at low SNR (single-particle electron
microscopy) and averaging of resonances of inter-atom distances of many
molecules in solution (nuclear magnetic resonance [NMR] analysis).
As detailed in Fig. 2.1 , NMR, X-ray and electron crystallography can
attain three-dimensional (3D) atomic resolution. However, to obtain
atomic resolution datasets these techniques imply merging of billions of
molecules. Furthermore, a series of biochemical procedures are needed
 
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