Dedicated to state-of-the-art time-resolved research in biological and physical sciences. Learn More About BioCARS

BioCARS

BioCARS micro-spectrophotometer for on-line and off-line recording of optical absorption spectra of crystals, to aid X-ray diffraction studies. Learn More About Macromolecular Crystallography

Micro-spectrophotometer

BioCARS ps laser system: Spectra Physics, Ti:Sapphire Spitfire Pro 5 (780nm, 2ps, 1kHz, 5mJ/pulse) and TOPAS OP Learn More About BioCARS Laser Lab

Laser Lab

BioCARS 14 ID beamline provides necessary infrastructure for conducting state-of-the-art time-resolved X-ray scattering studies with 100ps time resolution, both in biology and in physical sciences. Learn More About 14 ID Beamline

14-ID Beamline

Laue diffraction pattern collected at 14 ID from a Scapharca Inequivalvis tetrameric hemoglobin crystal, as part of 100ps time-resolved studies. Learn More About Time Resolved Crystallography

Laue X-ray diffraction pattern

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 experiments. Laser pulses initiate reactions in naturally photo-sensitive proteins or in other proteins that are used with a suitable caged compound. They can also be used to initiate temperature or pH jumps. The overall goal of such experiments is to understand basic biological processes in structural and dynamic terms, at the level down to atomic resolution (in case of crystallography) and on time scales from 100 picoseconds to seconds. Scientific problems addressed by BioCARS users advance the dynamic understanding of biological molecules and are fundamental to important biomedical problems, as well as of practical importance to both pharmaceutical and biotechnological industries.

BioCARS operates two Experimental Stations, embedded in a Biosafety Level 3 (BSL-3) Facility. This BSL-3 synchrotron-based capability is unique in the United States and permits safe studies of biohazardous materials such as pathogenic human viruses.
*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.

Latest News and Highlights

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Crystal-on-crystal chips for in situ serial diffraction at room temperature

(June 20, 2018) Recent developments in serial crystallography at X-ray free electron lasers (XFELs) and synchrotrons have been driven by two scientific goals in structural biology – first, static structure determination from nano or microcrystals of membrane proteins and large complexes that are difficult for conventional cryocrystallography, and second, direct observations of transient structural species in biochemical reactions at near atomic resolution.

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New BioCARS Director, Prof. Rama Ranganathan

(December 2017) Distinguished biophysicist Rama Ranganathan joined University of Chicago as a professor in the Department of Biochemistry and Molecular Biology and Institute for Molecular Engineering. He is the new Director of BioCARS facility and will also lead the new Center for Physics of Evolving Systems at the University of Chicago.

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Pink-beam serial crystallography

(November 2, 2017) Serial X-ray crystallography allows macromolecular structure determination at both X-ray free electron lasers (XFELs) and, more recently, synchrotron sources. The time resolution for serial synchrotron crystallography experiments has been limited to millisecond timescales with monochromatic beams. The polychromatic, “pink”, beam provides a more than two orders of magnitude increased photon flux and hence allows accessing much shorter timescales in diffraction experiments at synchrotron sources.

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Science Careers in Search of Women Conference, Tour of BioCARS

(May 2, 2017) As in previous years, BioCARS participated again in the ANL-hosted annual Science Careers in Search of Women Conference this year (Click here for more).

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BioCARS User Publication is One of 20 Most Read Articles in Structural Dynamics in 2016

(Feb 22, 2017) Time-resolved solution scattering studies of a homodimeric hemoglobin conducted at BioCARS 14-ID beamline linked the perturbation in the water cluster at the dimer interface to the kinetics and structures of intermediate states in this hemoglobin.

View on Structural Dynamics site

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New Technique Shocks Proteins Into Action

(Dec 6, 2016) For a protein to carry out its job—whether it be replicating DNA, metabolizing fuel, transporting biomolecules, or sending cell signals—its amino acids have to move in certain ways. The patterns of these internal motions aren’t always well understood because the tools available to study them are limited.

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Experimental Advance Offers First Glimpse of Biophysics of Vision

(May 6, 2016) In a groundbreaking experiment using the world’s fastest camera, a team of scientists led by the University of Wisconsin-Milwaukee documented the fundamental processes of a chemical reaction as they occurred in real time. This means seeing how proteins, the building blocks of life, work in a few quadrillionths of a second.

In a paper published May 5 in the journal Science, the researchers describe how they acquired images of the effect of light on a tiny crystallized protein.

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