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Our Mission
BioCARS is a national user facility for synchrotron-based, dynamic studies in structural biology, located at Sector 14 of the Advanced Photon Source, at Argonne National Laboratory. BioCARS is an integral part of the multi-disciplinary Center for Advanced Radiation Sources (CARS) run by the University of Chicago.
Structural biology at BioCARS is supported by the National Institute of General Medical Sciences of the National Institutes of Health under grant number P41 GM118217.
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 a number of photons per 100ps pulse approaching that of free electron lasers (such as the LCLS). Short X-ray pulses are synchronized with ps or ns laser pulses for conducting pump-probe time-resolved experiments. We are currently developing methods for serial Laue micro-crystallography to facilitate studies of irreversible reactions while minimizing sample consumption. We are also implementing electric-field jump as a method for reaction initiation and studies of protein dynamics. The overall goal of time-resolved experiments is to understand basic biological processes in structural and dynamics terms, on time scales from 100 picoseconds to seconds.
*As of February 6, 2017, BioCARS facility is decommissioned as a BSL-3 laboratory. BioCARS is now approved for research up to the BSL-2 level.
APS-U and BioCARS
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Recent Publications
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/)
Biju, L. M., Wang, C., Kang, W., Tom, I. P., Kumarapperuma, I., Yang, X., and Ren, Z. (2022)
On-chip Crystallization and Large-Scale Serial Diffraction at Room Temperature.
JoVE (Journal of Visualized Experiments) e63022.
(https://www.jove.com/t/63022/on-chip-crystallization-large-scale-serial-diffraction-at-room)
Li, J., Zhu, Y., Yu, H., Dai, B., Jun, Y.-S., and Zhang, F. (2021)
Microbially Synthesized Polymeric Amyloid Fiber Promotes β-Nanocrystal Formation and Displays Gigapascal Tensile Strength.
ACS Nano 15, 11843–11853.
(https://pubs.acs.org/doi/10.1021/acsnano.1c02944)
Carrillo, M. et al. (2021)
High-resolution crystal structures of transient intermediates in the phytochrome photocycle.
Structure 29, 743-754.e4.
(https://www.sciencedirect.com/science/article/pii/S0969212621000770)
Latest News and Highlights
BioCARS welcomes new staff member Eric Zoellner
Eric will be the new Beamline Mechanical Technician for Sector 14.
Light-Induced Protein Structural Dynamics in Bacteriophytochrome Revealed by Time-Resolved X-ray Solution Scattering
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.
On-chip Crystallization and Large-Scale Serial Diffraction at Room Temperature
Biju, L. M., Wang, C., Kang, W., Tom, I. P., Kumarapperuma, I., Yang, X., and Ren, Z. (2022) On-chip Crystallization and Large-Scale Serial Diffraction at Room Temperature. JoVE (Journal of Visualized Experiments) e63022.
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.
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.
