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

Using surface-bound rubidium ions for protein phasing.

S Korolev1, I Dementieva, R Sanishvili

  • 1Biosciences Division and Structural Biology Center, Argonne National Laboratory, 9700 South Cass Avenue, Building 202, Argonne, IL 60439, USA.

Acta Crystallographica. Section D, Biological Crystallography
|June 22, 2001
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

A funnel approach to enable analyses of epitope-specific human CD4 T cells specific for influenza and SARS-CoV-2.

mBio·2026
Same author

Evolutionary Adaptation of Prephenate Dehydrogenases: A regulatory ACT domain acquisition in ecological niche specialization.

bioRxiv : the preprint server for biology·2025
Same author

Validation of 3D cryoEM single-particle reconstruction correctness and handedness with Ewald's sphere correction.

Structural dynamics (Melville, N.Y.)·2025
Same author

Time-resolved β-lactam cleavage by L1 metallo-β-lactamase.

Nature communications·2022
Same author

A novel signal transduction protein: Combination of solute binding and tandem PAS-like sensor domains in one polypeptide chain.

Protein science : a publication of the Protein Society·2017
Same author

Advances in structural studies of recombination mediator proteins.

Biophysical chemistry·2016

Rubidium ions can determine protein structures. This study used rubidium anomalous scattering to phase the Thermus thermophilus hsp60 apical domain crystal structure, aiding macromolecular interaction studies.

Area of Science:

  • Structural biology
  • Biophysics
  • Biochemistry

Background:

  • Rubidium (Rb) is a monovalent metal ion.
  • It can act as a counterion in protein solutions.
  • Understanding metal ion interactions with macromolecules is crucial.

Purpose of the Study:

  • To determine the crystal structure of the hsp60 apical domain from Thermus thermophilus.
  • To investigate the utility of rubidium ions in protein structure phasing.
  • To study the interaction of monovalent metal ions with proteins.

Main Methods:

  • X-ray anomalous scattering was employed.
  • Multiple-wavelength anomalous dispersion (MAD) data were collected.
  • Phasing was performed using the SHARP program and automated model building with ARP/wARP.

Related Experiment Videos

Main Results:

  • The crystal structure of the hsp60 apical domain was determined.
  • One protein molecule binds one well-ordered and one poorly-ordered Rb atom.
  • Rubidium anomalous scattering proved effective for phasing.

Conclusions:

  • Bound rubidium ions can be utilized for protein structure determination.
  • This method facilitates the study of monovalent metal ion interactions with macromolecules.
  • Rubidium phasing offers a viable approach in structural biology.