Candidates for Vice President

 

 

 David Rose

Department of Biology

University of Waterloo, Canada

 

 

Martha Teeter

Professor Emerita (2006-), Chemistry Dept., Boston College, Boston, MA. Volunteer Clinical Faculty (2004-), UC Davis School of Medicine, Sacramento, CA

Education: BA, University of Pennsylvania (1977); DPhil, Oxford University  (1981) with David Phillips; Postdoc, MIT, with Greg Petsko.

Professional Activities: ACA: Canadian Rep on Council (2002-2005, 2011-2014), Chair, Canadian Division, Local Chair, Toronto (2009). Canadian Institutes for Health Research: Peer Review Committees, University Delegate for Waterloo, Peer Review for Canadian Cancer Society, Alberta Heritage and others. Graduate Coordinator and Interim Department Chair, University of Toronto (2000-2008), Department Chair, University of Waterloo since 2009.

Research Interests: Macromolecular crystallography, particularly when applied to glycoside hydrolases associated with human health and disease. For many years, my group has been involved in studies of enzymes of the eukaryotic N-glycosylation pathway, specifically Golgi a-mannosidase II and ER a-glucosidase I. We have also been studying the human intestinal glucosidases involved in the processing of nutritional starch.

Statement: For almost my entire career, the ACA has been my professional home. I have been to many other meetings, but the ACA is unique in the way its meetings combine methodology and results.  The meetings also provide a platform for cross-fertilization across all branches of diffraction science, interactions across sectors (academia, industry, government), and close contact with vendors. Among the priority areas that I would foster in this leadership position are:

Young scientists: Every generation of scientists has its obstacles. Research in general, including in our field, has, arguably, changed more in the last generation than ever before. Technological developments, front-and-center at ACA meetings, have opened new frontiers and deepened the questions that the next generation can address. At the same time, government-supported universities in most countries have shrinking budgets, job freezes or reductions, and underfunded infrastructure renewal. The private sector is in a state of constant flux. Government research laboratories are downsizing or changing focus. The ACA has historically been an important resource for early-career scientists to gain profile, present their research, make valuable contacts, and have discussions about establishing and maintaining a career in research. I would continue to feature the role of the YSSIG in meeting sessions and events, and in Council participation. They need our advice and encouragement now, more than ever.

Science Policy and Outreach: I group these together because they are so closely intertwined. It has never been more important for science to be seen and to be "relevant" to advancing the welfare of our countries. Professional societies have an important role to play in communicating to politicians and to the general public what science can do to improve our world. A big part of that role is to facilitate communication among ourselves and to synthesize a common vision and voice. ACA meetings provide important means to facilitate those discussions.

 

Education: BA, Wellesley College,  (1966), PhD, Penn State Univ. (1973) with Harry Allcock.  Postdoc in Biology, MIT (1974-1976) with Alex Rich  and at Naval Research Lab (1976-1977) with Wayne Hendrickson.

Professional Activities: ACA: Program Chair McMaster, Canada (1986); distributed bitnet news to ~5000 crystallographers (1988-1994); Chair BioMac SIG (1991); Service awards: (1990, 1994); Computing and Data Comm. (1990-1994, Chair '94). Chaired and organized numerous sessions (1984-2003).  IUCr: Organized a session Beijing (1993); member IUCr Commission on Electronic Pulbication;   US Editor IUCr World Directory (1995). Sabbatical: Max Planck Institut für Biophysik in Frankfurt, Ger. with Helmut Michel (1994-1995). Biophysical Society: Exec. Comm. (1988-1990);  Head, Molecular Biophysics subgroup (2004).  Plenary Speaker: Mexican Society of Crystallography, Hermosillo, Mexico, (2001).  Other: Many study sections and numerous grant and journal reviews.  66 publications from 1971 to 2011.

Research Interests:  As the daughter of a physical chemist, I am fascinated by how physical forces - electrostatic and van der Waals - guide molecular interactions.  My route to becoming a protein crystallographer was sinuous, and one that gave me appreciation of different fields of crystallography.

In high school, I strongly resisted science, because, well - my father was a chemist.  I did take chemistry at Wellesley College, however. It was the summer after sophomore year that decided me about chemistry.  I took an NSF Summer Research  Assistantship with Emily Dudek, a Wellesl ey inorganic chemistry professor.  At the time, I was struggling with deciding to major in music or in chemistry. But that summer, I fell in love with scientific research and that, as they say, was that.

My first crystallography teacher in graduate school at Penn State was Bob Newnham, a material scientist. I fondly remember homework problems solving 1D Patterson maps of minerals by hand.  Later I used the same problems to teach crystallography at Boston University and Boston College. 

Clathrates provided my first research window into diffraction research.  I was amazed to find cyclotriphosphazine catechol derivatives spontaneously recrystallized when placed next to a beaker of benzene. These inclusion compounds formed channels only when other molecules were around to fill them, pulling them from the gas into the crystalline phase. And I became an inorganic chemist - a non-metal, inorganic chemistry PhD.

From there, with an NCI fellowship to study shape fitting in polycyclic aromatics with DNA, I spent a summer with Helen Berman on the structure of a thymine dimer. Then, I headed to MIT to postdoc with Alex Rich and wound up switching to macromolecular crystallography - tRNA.  Not trusting any molecule that I couldn't understand and visualize every atom of, I determined to eat my lunch next to an 8'X10' tRNA Richard's Box (electron density on plastic sheets with a molecular model fit to the density via a half silvered mirror and model supported by metal rods and piano wire), until I could trace the chain and make sense of it. It was a strange new world for me.

Quite accidentally, when fellow postoc Fran Jurnak and I were looking for a possible protein to crystallize, my attention was caught by a protein diffraction pattern in the article next to the one I was looking up in the Journal of Phytochemistry.   That launched me into the protein I have worked on for most of my career - crambin from Ethiopian cabbage.

Water, which forms clathrates in its own right, has always intrigued me.  And crambin crystals, although a 46-residue hydrophobic protein, contain about 30% water. The structure provides an excellent window into water structure around proteins.  Synchrotron data from crambin crystals diffract x-rays to 0.48 Å resolution (the smallest d spacing). This is the world's limit for protein crystals, to my knowledge.  Water positions, both single and doubled, are apparent, as well as bonding electron density. Likewise, multiple side chain conformations are found and these can be correlated to water positions.  Multiple temperature studies of these crystals provide evidence for a protein glass transition where not only correlated motion of side chains with water but also protein function ceases.  Thus, both this research and my additional studies on myoglobin crystals gave crystallographic evidence for the role of correlated substates as critical for protein function.  While others such as Greg Petsko had postulated this, I was able to show it at an atomic level.  It is these dynamic interactions I find truly fascinating.  I continue to research water structure around proteins in retirement.

Graphics - both movies and illustrations of molecular models - have always played a key role in my teaching and research, from making undergraduate lab demos in graduate school to shooting movies of crambin for research to constructing figures for publication.  I have continued to explore the visual arts in retirement.  I made a short documentary, which was among the top ten at a Sacramento Film Festival in 2008.  I have hosted and/or produced over 20 1/2 hour interview shows on our local cable station in Davis, as well as several longer productions.  My particular favorite was "Teaching College Science through Song".  It was an interview with a friend and colleague, a plant, water and soil scientist, who is part of the Art-Science Fusion program at UC Davis as well as a songwriter herself.  In her class, students in groups write songs about science and perform them at a public venue.  Their songs are about such topics as the water cycle, how soil is formed, and the like.

Teaching is also an important part of my retirement.  I teach an applied seminar at UC Davis Medical School. I find it both rewarding and challenging.  Spending time to help students learn to think logically, put their clinical learning with basic biochemical principles, and learn to work together on a case is very satisfying. I believe that education in science is something we must take time for at every level possible.

Statement: The IUCr has proclaimed 2014 the International Year of Crystallography (IYCr), in honor of the discovery of x-ray diffraction by Von Laue and the Braggs (father and son). UNESCO and the International Council for Science support this centennial.  What an exciting time to be a crystallographer!  Proposed IUCr aims for this year include: To increase the public awareness of crystallography; to increase the awareness of the way crystallography underpins most of the technological developments in our modern society; to illustrate the universality of science; to increase the awareness of the way crystallography underpins investigations of cultural heritage artifacts; and to promote education in crystallography and its links to other sciences

As a crystallographer and science educator, I am keenly aware of an anti-science attitude among certain political candidates, corporations and their think tanks, and anti-science educators.  I think crystallography provides wonderful opportunities to develop an awe of the natural world and the scientific method for children and adults.  For years, I used crystallization in gels demonstrations from the Hauptman-Woodward Institute with elementary and college students alike.  I have also used Marge Kastner's program for explaining space groups and many other visual tools for teaching diffraction, such as simulations of interference between two slits.  I am an advocate for multi-disciplinary approaches to teaching science as well as for scientific research.  I would advocate for the many disciplines of crystallography represented in the ACA. 

This juxtaposition of IYCr with anti-science trends presents tremendous opportunities to use crystallography to increase public and political awareness of science and its benefits.  I would make this a major emphasis in my term serving the ACA.  I envision enabling creation of a series of both short and longer videos and visual aids to bring crystallography before the world and document the accomplishments of diffraction, curriculum units for science teachers to professors, and creation of material to help politicians understand science and its contributions.  I hope to elicit the creativity of old and young crystallographers in bringing this message to the world.  Further, the IUCr is scheduled for Montreal in 2014, which provides an additional forum to not only hold a symposium on 100 years of diffraction but also to publicize and bring to world attention the accomplishments and the promises for diffraction and for science in solving problems.

Funding for crystallographic research, which is very often interdisciplinary, is another priority for me. I hope to listen and learn from current and past councilors as to other issues facing the ACA at this juncture.

Nomination for VP is a great honor and a chance for me to give back to a society that has provided much for me.  Crystallography has been much more than my livelihood.  The ACA provided my first professional opportunities to attend international meetings (yes, I was one of those graduate students in 1969 lucky enough to attend the IUCr in Stony Brook on scholarship and show slides for the sessions) and has continued to provide a forum for critical and supportive advances in all levels of crystallography for me.  I remember Jim Ibers providing that feedback when I was an outspoken graduate student.  Wayne Hendrickson was patient and inventive with this odd crystal crambin, and in the '80's, Håkon Hope cooled a crambin crystal to liquid nitrogen temperatures, as he had done with Ada Yonath's early ribosome crystals.  There are too many important people to mention that have mentored me.  I am thrilled to have the opportunity to represent a discipline of creative, honest individuals,  curious about the science and inventing new crystallographic and computational tools to solve problems.  This is a great time to share crystallography with the world