BioCARS: A Synchrotron Structural Biology Resource

BioCARS: A Synchrotron Structural Biology Resource

Research Emphasis

BioCARS, a component of the Consortium for Advanced Radiation Sources (CARS), is operating Sector 14 at the Advanced Photon Source at Argonne National Laboratory as a national user facility for synchrotron radiation research. The scientific interests of BioCARS are crystallographic studies of viruses, ribosomes, and other complexes with very large unit cells; studies of microcrystals; time-resolved crystallography; and scattering from less-ordered biological systems. In all cases, the goal is to understand basic biological processes in structural terms, a goal fundamental to the pharmaceutical and biotechnology industries as well as to basic science.

Current Research

Design, construction and installation of novel optical elements to deliver the brilliant X-ray beam to the crystals; design and construction of all components necessary to upgrade one sector at the Advanced Photon Source consisting of one insertion device and one bending magnet beamline, with three experimental stations; strategies for the effective acquisition of time-resolved data and its analysis, and the acquisition of precise MAD data; spectroscopic, static and time-resolved studies of single crystals of biological photoreceptors; and studies of single crystals of materials classified as Biosafety Level 2 and 3 substances (BSL-2 and BSL-3).

Resource Capabilities

Methods

Static and time-resolved X-ray diffraction on single crystals using monochromatic and polychromatic synchrotron radiation; associated single crystal absorption spectroscopy and pulsed laser illumination. As a unique feature, the resource is embedded in a Biosafety Level 3 facility that permits safe operation of all experimental stations and control areas in BSL-2 or BSL-3 modes.

Instruments

Appropriate hardware for experiments in all areas outlined.

Software

Appropriate software to control experiments in all areas outlined; to permit data reduction to structure amplitudes for both monochromatic and polychromatic, Laue data; and to permit phase determination and refinement.

Special Features

The resource is unique in offering the capability to conduct experiments on single crystals of biohazards that require BSL-2 and BSL-3 containment; and is unique in the United States in offering the capability for nanosecond and, in the near future, 100ps time-resolved macromolecular crystallography.

Training Opportunities and Workshops

The center offer extensive, hands-on training in the use of the experimental stations and in data acquisition and reduction to all users.

Publications

Users of BioCARS publish over 100 peer-reviewed journal articles per year. View the BioCARS Publication List.

1. Ihee, H., Rajagopal, S., Srajer, V., Pahl, R., Anderson, S., Schmidt, M., Schotte, F., Anfinrud, P. A., Wulff, M., and Moffat, K., Visualizing reaction pathways in photoactive yellow protein from nanoseconds to seconds. Proceedings of the National Academy Sciences, USA 102:7145–7150, 2005.

2. Liu, D., Lepore, B. W., Petsko, G. A., Thomas, P., W., Stone, E., M., Fast, W., Ringe, D., Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis. Proceedings of the National Academy Sciences, USA 102:11882–11887, 2005.

3. Terrak, M., Rebowski, G., Lu, R. C., Grabarek, Z., and Dominguez, R., Structure of the light chain-binding domain of myosin V. Proceedings of the National Academy Sciences, USA 102:12718–12723, 2005.

4. Xia, C., Bator-Kelly, C. M., Rieder, E., Chipman, P. R., Craig, A., Kuhn, R. J., Wimmer, E., and Rossmann, M. G., The Crystal Structure of Coxsackievirus A21 and Its Interaction with ICAM-1. Structure 13:1019–1033, 2005.