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Our Science – MCL Website

Macromolecular Crystallography Laboratory

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In addition to the information presented below, the MCL has an alternative website that can provide you with more detail about their work.

Overview

The interests of the Laboratory cover a wide range of systems and techniques relevant to macromolecular crystallography and its applications. The Synchrotron Radiation Research Section, based at the Advanced Photon Source at Argonne National Laboratory and headed by Dr. Zbigniew Dauter, is involved in developing new macromolecular crystallography methods related to the tunability and high intensity of synchrotron radiation, such as the use of anomalous signals, particularly from comparatively light atoms, and the effects of radiation damage incurred in crystals of proteins. This Section has also been involved in collaborative efforts with a number of groups within and outside MCL in extending the resolution of crystal structures of proteins and nucleic acids to atomic levels and in investigating parameters which would define these structures as "high quality". The principal interest of Dr. Xinhua Ji's Biomolecular Structure Section is the structure and mechanism of biomolecular systems with anticancer and/or antimicrobial significance and structure-based drug design targeting such biomolecules. Systems under investigation include RNA-processing proteins, RNA polymerase-associated transcription factors, folate pathway enzymes, and detoxification enzymes. The Protein Engineering Section, headed by Dr. David Waugh, develops and refines methods for high-throughput protein expression and purification, and engages in structure-assisted drug design with particular emphasis on proteins involved in cancer. Under the direction of Dr. Alexander Wlodawer, the Protein Structure Section is involved in investigating a variety of proteases, with particular emphasis on viral enzymes, retropepsins; lectins with antiviral activity; complexes of antibodies with antigens; and a number of cytokines and cytokine-receptor complexes. PSS is also involved in collaborative studies of C/EBP transcriptional activators and in computational investigations of enzymatic mechanisms of proteases.

This page was last updated on 2/7/2013.