Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Biological cryo atomic force microscopy: a brief review

Z Shao1, Y Zhang

  • 1Department of Molecular Physiology, University of Virginia School of Medicine 22908, USA. zs9q@virginia.edu

Ultramicroscopy
|December 1, 1996
PubMed
Summary

Cryogenic atomic force microscopy (cryo-AFM) overcomes limitations of room-temperature imaging for soft biological molecules. This technique achieves high resolution, revealing unique structural information previously inaccessible.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The effects of K+ channel blockers on the spontaneous electrical and contractile activity in the proximal renal pelvis of the guinea pig.

The Journal of urology·1996
Same author

Interferon-gamma inhibits HIV-induced invasiveness of monocytes.

Journal of leukocyte biology·1995
Same author

Phosphorylation of Raf by ceramide-activated protein kinase.

Nature·1995
Same author

Cyclin D3 is essential for megakaryocytopoiesis.

Blood·1995
Same author

A P2X purinoceptor cDNA conferring a novel pharmacological profile.

FEBS letters·1995
Same author

Phosphorylation of nodulin 26 on serine 262 affects its voltage-sensitive channel activity in planar lipid bilayers.

The Journal of biological chemistry·1995

Area of Science:

  • Biophysics
  • Structural Biology
  • Microscopy

Background:

  • Atomic force microscopy (AFM) faces challenges with biological specimens due to molecular softness and thermal motion.
  • Imaging flexible multi-domain or multi-subunit molecules at room temperature is particularly difficult.

Purpose of the Study:

  • To review the instrumentation and biological applications of cryogenic atomic force microscopy (cryo-AFM).
  • To highlight cryo-AFM's capability to overcome limitations of traditional AFM for biological samples.

Main Methods:

  • Utilizing an AFM operated in liquid nitrogen vapor under ambient pressure.
  • Imaging biological specimens at cryogenic temperatures to mitigate thermal motion and sample deformation.

Main Results:

Related Experiment Videos

  • Cryo-AFM successfully imaged biological specimens that were poorly resolved at room temperature.
  • High-resolution imaging was achieved, providing potentially important structural insights.
  • Demonstrated versatility and unique capabilities of cryo-AFM in structural biology.

Conclusions:

  • Cryo-AFM is a powerful tool for high-resolution imaging of challenging biological structures.
  • The technique overcomes key limitations of room-temperature AFM for soft biological molecules.
  • Cryo-AFM offers unique capabilities and establishes itself as a versatile structural probe in biology.