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Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
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.
Summary
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.
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.
