News Release

Edited versions of this article, written by Dr. Kenneth Taylor, appeared in the January 7 edition of the Tallahassee Democrat newspaper and Volume 33, Number 11 of State: a Bulletin for the Faculty and Staff of Florida State University.

More than 100 scientists from across the United States, Europe, Japan, Venezuela and as far away as the People's Republic of China - the world's top experts on the structure of molecules - will converge at the Turnbull Center on Friday and Saturday, Jan. 8 and 9, for the Second Structural Biology Symposium hosted by the Florida State University Institute of Molecular Biophysics and Structural Biology Program. The symposium celebrates "25 years of CryoElectron Microscopy of Biological Macromolecules" and focuses on imaging of macromolecular structures using high resolution electron microscopy.

"Unique, advanced, electron microscopes, such as the one now used by FSU scientists in the Structural Biology Program, are helping us to solve mysteries of the structure of proteins, research that could lead to a better understanding of cancer, for example," said Professor Kenneth Taylor of the FSU Department of Biological Science. "That will be the common theme of our symposium." The symposium has attracted speakers from around the world who were instrumental in developing the technique and who are extending the method to ever higher resolutions and solving ever more complex structures.

The techniques used in these studies were pioneered 25 years ago by Prof. Robert Glaeser of the University of California, the keynote speaker at the symposium and a long time advocate of high resolution electron microscopy in structural biology. One of the unique aspects of electron microscopy is its ability to image biological structure over a wide resolution range, from atomic resolution imaging of crystals, to lower resolution images of whole cells but at much higher resolution than possible by light microscopy. This characteristic has enabled electron microscopy to have a wide impact in many areas of structural biology including the study of membrane proteins, viruses, large macromolecular complexes, the molecules and filaments of the cytoskeleton and most recently, 3-D images of whole bacteria. The advent of cryoelectron microscopy allowed investigators to study these structures in a native state, frozen in a thin layer of "glassy", that is to say, noncrystalline ice.

Dr. Jacques Dubochet made the key discovery of the methodology for freezing specimens in a thin, glassy ice film and has continued to use the methodology to study the structure of nucleic acids. Dr. Wolfgang Baumeister (Max Planck, Martinsried, Germany) is the world leader in the development of 3-D imaging of whole bacteria frozen in glassy ice. High resolution electron microscopy has been instrumental in studying the cytoskeleton and the molecular mechanisms of molecular motors. Several speakers, Drs. Ron Milligan (Scripps Research Institute, La Jolla, CA, Michael Reedy (Duke University) and Keiko Hirose (Japan) are making key advances by showing the structure of these motors in their different states. One of the speakers, Dr. Ken Downing of the University of California at Berkeley, has recently solved the structure of tubulin, the molecular target of the anticancer drug, taxol using electron microscopy. Dr. R. A. Crowther from the Medical Research Council Laboratory of Molecular Biology in Cambridge, England was instrumental in the development of methods to image individual virus particles in 3-D and whose laboratory currently holds the record for a high resolution virus structure by electron microscopy. Dr. Stephen Fuller will present work on the structure of the AIDS virus. Dr. Andreas Engel (U. Basel, Switzerland) has solved the structure of the water channel, a key protein in the function of the kidney and has been instrumental in the development of membrane protein crystallization methods for electron microscopy. Dr. Vinzenz Unger (Max Planck, Frankfurt, Germany) has crystallized and solved the structure of the communicating intercellular junction, a protein that plays a major role in heart muscle contraction. Several of the newer investigators, Drs. Karen Williams (Max Planck, Frankfurt, Germany) and Manfred Auer (Skirball Inst., New York) have made major advances in the study of membrane transport proteins which play an important role in nutrient absorption. Drs. Alain Brisson (Univ. of Groningan, The Netherlands) and Kenneth Taylor (FSU) us lipid monolayers to study cytoskeletal proteins and their interactions with membrane lipids.

Earlier in the week, in a short ceremony at noon on Thursday in Room 555 of the Molecular Biophysics Building, FSU will dedicate its $1,300,000 microscope facility, made possible by two $400,000 grants, one from the National Institutes of Health and the other from the National Science Foundation and matching funds from the Markey Foundation and FSU.

Florida State is the first university in the world to have this particular type of microscope dedicated to structural biology. The establishment of this facility within the Structural Biology Program allows FSU researchers to study a wide range of structural problems ranging from the action of molecular motors in muscle, the structure of cytoskeletal proteins, cell adhesion, virus structure and antigen-antibody interaction. The program is thus uniquely equipped to combine the three major techniques of structural analysis, X-ray crystallography, multidimensional NMR and high resolution electron microscopy, in the study of the molecular mechanisms that underlie human disease.