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Our Mission
The mission of BioCARS is to provide state-of-the-art X-ray facility, scientific and technical expertise and support to enable users to study the dynamic properties of biological macromolecules by X-ray scattering techniques: time-resolved diffraction and solution scattering (SAXS/WAXS). In hybrid mode of the APS storage ring, BioCARS 14-ID beamline provides high polychromatic flux, with ~3 × 1010 photons per 100ps pulse delivered to the sample. Short X-ray pulses are synchronized with ps or ns laser pulses for conducting pump-probe time-resolved experiments. In recent years we developed and implemented these technologies that are now offered as standard methods to BioCARS users:
- Serial Laue micro-crystallography using fixed targets and crystal injectors to facilitate studies of irreversible reactions while minimizing sample consumption.
- Electric-field jump as a method for reaction initiation and studies of protein dynamics.
- Novel temperature-controlled sample cells for temperature-jump solution scattering studies.
- Sample-minimizing co-flow cell for time-resolved solution scattering studies of irreversible reactions.
The overall goal of time-resolved experiments at BioCARS is to understand basic biological processes in structural and dynamics terms, on time scales from 100 picoseconds to seconds.
Use of BioCARS is supported by the National Institute of General Medical Sciences of the National Institutes of Health under grant number P41 GM118217. Funding acknowledgement for publications resulting from use of BioCARS facility can be found here.
APS-U and BioCARS
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Recent Publications
Chan, A. M., Nijhawan, A. K., Hsu, D. J., Leshchev, D., Rimmerman, D., Kosheleva, I., Kohlstedt, K. L., and Chen, L. X.
The Role of Transient Intermediate Structures in the Unfolding of the Trp-Cage Fast-Folding Protein: Generating Ensembles from Time-Resolved X-ray Solution Scattering with Genetic Algorithms.
J. Phys. Chem. Lett. 14, 1133–1139 (2023).
(https://pubs.acs.org/doi/10.1021/acs.jpclett.2c03680)
Dalton, K. M., Greisman, J. B., and Hekstra, D. R.
A unifying Bayesian framework for merging X-ray diffraction data.
Nat Commun 13, 7764 (2022).
(https://www.nature.com/articles/s41467-022-35280-8)
Wilamowski, M., Sherrell, D. A., Kim, Y., Lavens, A., Henning, R. W., Lazarski, K., Shigemoto, A., Endres, M., Maltseva, N., Babnigg, G., Burdette, S. C., Srajer, V., and Joachimiak, A.
Time-resolved β-lactam cleavage by L1 metallo-β-lactamase.
Nat Commun 13, 7379 (2022).
(https://www.nature.com/articles/s41467-022-35029-3)
Lee, S. J., Kim, T. W., Kim, J. G., Yang, C., Yun, S. R., Kim, C., Ren, Z., Kumarapperuma, I., Kuk, J., Moffat, K., Yang, X., and Ihee, H. (2022)
Light-induced protein structural dynamics in bacteriophytochrome revealed by time-resolved x-ray solution scattering.
Science Advances 8, eabm6278.
(https://www.science.org/doi/10.1126/sciadv.abm6278)
Moreno-Chicano et al. (2022)
Complementarity of neutron, XFEL and synchrotron crystallography for defining the structures of metalloenzymes at room temperature.
IUCrJ 9, 610–624.
(https://journals.iucr.org/m/issues/2022/05/00/rs5001/)
Latest News and Highlights
See also: APS Science Highlights
Time-Resolved X-ray Scattering Studies of Proteins
Cho, H. S., Schotte, F., Stadnytskyi, V., and Anfinrud, P. (2021) Time-resolved X-ray scattering studies of proteins.
Current Opinion in Structural Biology 70, 99–107.
Effect of the Abolition of Intersubunit Salt Bridges on Allosteric Protein Structural Dynamics
Choi, M., Kim, J. G., Muniyappan, S., Kim, H., Kim, T. W., Lee, Y., Lee, S. J., Kim, S. O., and Ihee, H. (2021) Effect of the abolition of intersubunit salt bridges on allosteric protein structural dynamics.
Chem. Sci. 12, 8207–8217
2021 APS Users Meeting – Workshop: Dynamic X-ray Crystallography
BioCARS staff Robert Henning, together with APS GM/CA and SBC-CAT staff, organized Dynamic X-ray Crystallography workshop at the 2021 APS Users Meeting.
Unfolding Bovine α-Lactalbumin with T-Jump: Characterizing Disordered Intermediates via Time-Resolved X-Ray Solution Scattering and Molecular Dynamics Simulations
Hsu, D. J., Leshchev, D., Kosheleva, I., Kohlstedt, K. L., and Chen, L. X. (2021)
Unfolding bovine α-lactalbumin with T-jump: Characterizing disordered intermediates via time-resolved x-ray solution scattering and molecular dynamics simulations.
J. Chem. Phys. 154, 105101.
An Automated Platform for in Situ Serial Crystallography at Room Temperature
Ren, Z., Wang, C., Shin, H., Bandara, S., Kumarapperuma, I., Ren, M. Y., Kang, W., and Yang, X. (2020) An automated platform for in situ serial crystallography at room temperature. IUCrJ 7.
BioCARS Starts a New Zoom Seminar Series
During these times of COVID-19 restrictions, when most BioCARS users cannot travel to BioCARS to conduct their experiments, we deemed it essential to continue regular communications and scientific discussions with our user community. We decided to start BioCARS Zoom...
Sample-minimizing co-flow cell for time-resolved pump–probe X-ray solution scattering
Kosheleva, I., Henning, R., Kim, I., Kim, S. O., Kusel, M., and Srajer, V.
Time-resolved β-lactam cleavage by L1 metallo-β-lactamase
Wilamowski, M., Sherrell, D. A., Kim, Y., Lavens, A., Henning, R. W., Lazarski, K., Shigemoto, A., Endres, M., Maltseva, N., Babnigg, G., Burdette, S. C., Srajer, V., and Joachimiak, A. (2022) Time-resolved β-lactam cleavage by L1 metallo-β-lactamase. Nat Commun 13, 7379.