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

Macromolecular structure determination by cryo-electron microscopy.

H R Saibil1

  • 1Department of Crystallography, Birkbeck College, Malet Street, London WC1E 7HX, England. h.saibil@mail.cryst.bbk.ac.uk

Acta Crystallographica. Section D, Biological Crystallography
|September 22, 2000
PubMed
Summary
This summary is machine-generated.

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

Structural analysis of macromolecular assemblies by electron microscopy.

Chemical reviews·2011
Same author

Chaperonin complex with a newly folded protein encapsulated in the folding chamber.

Nature·2009
Same author

Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding.

Advances in protein chemistry·2002
Same author

Three-dimensional structure of an invertebrate rhodopsin and basis for ordered alignment in the photoreceptor membrane.

Journal of molecular biology·2002
Same author

ATP-bound states of GroEL captured by cryo-electron microscopy.

Cell·2002
Same author

Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy.

Journal of structural biology·2001
Same journal

Structural insights into the synthesis of FMN in prokaryotic organisms.

Acta crystallographica. Section D, Biological crystallography·2015
Same journal

Native sulfur/chlorine SAD phasing for serial femtosecond crystallography.

Acta crystallographica. Section D, Biological crystallography·2015
Same journal

Serial crystallographic analysis of protein isomorphous replacement data from a mixture of native and derivative microcrystals.

Acta crystallographica. Section D, Biological crystallography·2015
Same journal

The first crystal structure of the peptidase domain of the U32 peptidase family.

Acta crystallographica. Section D, Biological crystallography·2015
Same journal

Atomic resolution crystal structure of Sapp2p, a secreted aspartic protease from Candida parapsilosis.

Acta crystallographica. Section D, Biological crystallography·2015
Same journal

Structural characterization of a mitochondrial 3-ketoacyl-CoA (T1)-like thiolase from Mycobacterium smegmatis.

Acta crystallographica. Section D, Biological crystallography·2015
See all related articles

Recent advances in cryo-electron microscopy (cryo-EM) hardware and software now make it a powerful tool for determining macromolecular structures. This technique complements X-ray crystallography and NMR, especially for large biological assemblies.

Area of Science:

  • Structural biology
  • Biophysics
  • Microscopy

Background:

  • X-ray crystallography and NMR are established methods for macromolecular structure determination.
  • Limitations exist for these techniques, particularly for large and complex biological assemblies.

Purpose of the Study:

  • To review recent advances in cryo-electron microscopy (cryo-EM).
  • To survey the capabilities of cryo-EM for macromolecular structure determination.
  • To highlight cryo-EM as a complementary technique to X-ray crystallography and NMR.

Main Methods:

  • Improvements in transmission electron microscopy (EM) hardware.
  • Advancements in low-temperature sample preparation methods.
  • Development of sophisticated image-processing software.

Related Experiment Videos

Main Results:

  • Cryo-EM has become a crucial technique for determining the structure of macromolecules.
  • The technique is particularly effective for analyzing large molecular assemblies.
  • Cryo-EM offers a powerful alternative and complement to traditional methods.

Conclusions:

  • Recent technological progress has significantly enhanced the capabilities of cryo-EM.
  • Cryo-EM is now a vital tool in structural biology, expanding the scope of molecular structure determination.