We teamed up with our crystallography and small angle scattering colleagues in ALS-ENABLE to characterize the SpyCatcher-SpyTag system using all three methods in the P30 Center.
We describe here our new capability combining X-ray footprinting with in-line FRET spectroscopy.
X-ray footprinting was used in this study to validate the AlphaFold2 model of enzyme binding to a bacterial microcompartment tile protein.
We validated the interaction of the monoclonal antibody nivolumab with its antigen target PD-1 using X-ray footprinting.
X-ray footprinting experimental data was used to corroborate molecular simulations of permeability in bacterial microsome shell proteins.
Our collaborator M. Gochin used several biochemical and structural methods, including X-ray footprinting and crystallography, to investigate the structures and possible mechanisms of potency of gp41 fusion proteins toward HIV inactivation.
Using high-dose rate radiation "FLASH radiation" to treat cancer is emerging as a promising new avenue in oncology. In this paper we present a new platform for comparing high dose rate and low dose rate radiation effects on peptides in solution at a fundamental level.
Investigating the use of cell penetrating peptides to introduce SpyCatcher into cells for labeling or imaging studies.
A mini-review of how hydroxyl radical footprinting can be applied for investigation of antibody structure.
Description of our sample jet delivery system implemented at the 3.3.1 endstation.
A concept for hybrid measurement of global fluorescence and residue-specific footprinting, as applied specifically to study amyloid beta aggregation.
Low dissolved oxygen in solution leads to less overall modification of proteins, and some interesting differences in the modification profiles.
Our collaborators in the Craik group used footprinting to investigate antibodies against uPA, a biomarker of aggressive cancers.
A brief overview of combining multiple structural methods to understand carotenoid-protein interactions.
Our collaborators used footprinting along with crystallography and cryoEM to investigate a new nanobody against the famous virus.
A nice combination of SAXS and XFMS to investigate how a carotenoid is bound within a protein, and the effect on oligomeric structure.
XFMS and molecular dynamics combined to investigate how a bacterial motor protein functions.
Our collaborators from the NSLS-II footprinting beamline used our beamline to help figure out a new footprinting method using CF3.
Description of our new jet sample delivery system, and how it compares to standard sample delivery systems for XFMS.
Here we combined crystallography, spectroscopy, and XFMS to delineate the differences between homologous forms of the Orange Carotenoid protein.
Our collaborators used our beamline to investigate a protein-DNA binding interaction, and how that regulates telomere length.
We used XFMS to determine the sequence of events in photoactivation of the Orange Carotenoid Protein and its de-activation by the Fluorescence Recovery Protein.
XFMS was used to determine interaction regions between proteins that make up bacterial microcompartment shells.
Latest updates in XFMS instrumentation at the ALS, as of 2019. (More recent updates are in articles listed above.)
XFMS was used to help work out the water-mediated transport of Zn through a bacterial ion channel.
A brief review of how XFMS can be helpful in characterizing structure and function of membrane proteins.
Our collaborators used XFMS, SAXS, and computational modeling to determine the ensemble structure of the transactivation domain of a human estrogen receptor.
Selected publications prior to 2019
XFMS, SAXS, and computational modeling were used together to determine the architecture of a human estrogen receptor.
We used XFMS to determine the sites of interaction between metal nanoparticles and an iron-binding protein. A Berkeley news release about the work can be found here.
We used XFMS and crystallography to show that the carotenoid molecule within the Orange Carotenoid Protein makes a very large shift within protein domains upon photoactivation. A Berkeley news release about the work can be found here.
We used XFMS, crystallography, SAXS, and HDX-MS to investigate conformational changes in the Orange Carotenoid Protein during photoactivation.
Our very first paper from the newly developed footprinting beamline at the ALS.
This is the first paper demonstrating that X-ray footprinting could be done at a synchrotron other than the NSLS.
