2016 ACA Trueblood Award to Axel Brunger

The 2016 Trueblood Award of the American Crystallographic Association for "exceptional achievements in computational or chemical crystallography" will be bestowed on ACA member Axel Brunger, Professor of Molecular and Cellular Physiology, Neurology and Neurological Sciences, Structural Biology (by Courtesy), and Photon Science Investigator, at the Howard Hughes Medical Institute at Stanford University.

 

Brunger carried out his undergraduate studies in Germany, between Hamburg and Munich, where he received a PhD in biophysics from the Technical University. He then moved to Harvard, to work as a post-doctoral researcher in the group of Martin Karplus. He very quickly became Associate Professor in Biophysics at Yale and progressed steadily in his academic career. In parallel, he also became investigator at the Howard Hughes Medical Institute, to which he has been affiliated since 1995.

 

Axel's contribution to computational crystallography has been invaluable for the development of modern macromolecular crystallography. It was very early in his career, when he was only a post-doctoral fellow, that he developed algorithms based on simulated annealing and molecular dynamics to refine protein structures. With John Kuriyan and Martin Karplus, he implemented these methods into the program XPLOR, which he later expanded into the widely used CNS, a freely available software that includes optimized tools for structure refinement, phasing and molecular replacement.

 

To prevent the possibility of over-refinement of crystallographic structures using simulated annealing, Brunger borrowed a cross-validation approach from statistics and adapted it to protein crystallography: the free R factor. This is now the standard criterion to judge agreement between observed and calculated structure factors. Also, in collaboration with Michael Levitt, Axel developed the DEN method (for Distortable Elastic Network), a refinement strategy that uses flexible adjustable restraints and that allows low-resolution refinements. His powerful computational tools revolutionized structural calculation, moving it towards automation and allowing non-experts to gain access to protein crystallography.

 

His brilliant contributions were all born as solutions to complex structural problems at the forefront of scientific investigation. Today Brunger is still pushing the limits of structural biology. He carries out cutting-edge research on the structural mechanisms of synaptic neurotransmitter release, complementing x-ray crystallography with single molecule microscopy and is exploring the new possibilities that x-ray free electron laser techniques offer for the structural determination of large macromolecular assemblies.

 

The award presentation and lecture is scheduled for Saturday, July 23, at 8:00am.

 

 

2016 ACA Fankuchen Award to Elspeth Garman

The ACA will bestow the 2016 Fankuchen Award on Elspeth Garman, from Oxford University, UK. The award, which has been created "to recognize contributions to crystallographic research by one who is known to be an effective teacher of crystallography," honors Elspeth's absolute dedication to teaching crystallography in seminars and workshops all over the world, and her great contributions to improve cryo-methods in crystallography.

 

Elspeth graduated in nuclear physics from Oxford University in 1979 and switched to biochemistry only later in her career, in 1987, when she joined the research staff at the Laboratory of Molecular Biophysics in Oxford. Since 1999 she has been faculty at the biochemistry department at Oxford University, where she now holds a position as Professor of Molecular Biophysics and as Director of the Systems Biology Programme at the Doctoral Training Centre. She is also Nicholas Kurti Senior Research Fellow in Macromolecular Crystallography and Tutor for Graduates at Brasenose College.

 

Elspeth's research on cryo-cooling and radiation damage has had a profound impact on crystallography. Armed with a rigorous approach inherited from her physics background and her natural inventiveness, she optimized cryogenic tools and cooling parameters, introducing a methodical approach to cryo-cooling that greatly improved diffraction data. Since radiation damage emerged as a serious problem in crystallographic structure calculation in 2000, she has spearheaded the studies dedicated to the issue, introducing mitigating measures such as the use of small molecules as radical scavengers. She experimentally determined the maximum x-ray dose that can be delivered to a macromolecule before compromising its structure—a parameter that is now called "the Garman" limit—and presented a method to predict the lifetime of proteins exposed to certain radiation doses. She also pioneered the use of an online UV-visible spectrometer to detect the early signs of radiation damage. Besides these studies, she developed the proton induced x-ray emission (PIXE) technique, which allows precise identification of trace metal elements within a protein structure, and she determined the structure of many proteins involved in infectious diseases.

 

Elspeth's value as a teacher and as a lecturer is appreciated at large. She is a very popular speaker at workshops all over the world, and her passion and enthusiasm for crystallography have left a long-lasting impression on her students and on her colleagues alike. She has tutored on 75 international courses, given 117 scientific lectures and 41 public lectures on crystallography, and organized 18 workshops. From 2009 to 2012 she was President of the British Crystallographic Association and from 2007-2011 she served as an Auditor of the European Crystallographic Association. The University of Oxford recognized her teaching qualities with the `Major Educator' personal teaching award in 2008; in 2014 she received the Most Acclaimed Lecturer Award for the Medical Sciences Division from the Oxford University Students Union. She is deeply involved in outreach programs aimed at increasing public scientific awareness both in a young and in an adult audience. For many years she has lectured at "Girls into Physics" conferences and she is often invited to give talks in schools all over the UK. She has been a speaker at the Royal Institution multiple times, and last year she delivered a public lecture at the Royal Albert Hall in occasion of the International Year of Crystallography. She is very comfortable with the media and the press: she has participated in over 40 TV and radio programmes and she has been often quoted in the main UK newspapers. In one of her most recent media appearances, an interview for the program "The Life Scientific" broadcasted by BBC4 in October 2014, she spoke at length about crystallography, about her life-long journey into experimental science...and about using her baby's hair to build the first cryo-loops. It is a most enjoyable conversation, which sums up her self-less attitude towards research and her desire to fuel progress in crystallography and in science in general; you can listen to it here: www.bbc.co.uk/programmes/b04kbjhg.

 

The award presentation and lecture is scheduled for Tuesday, July 26, at 8:00am.

 

 

2016 ACA Bau Award to Benno Shoenborn

Benno Shoenborn, from Los Alamos National Laboratory, is the 2016 recipient of the ACA Bau Neutron Diffraction Award for his pioneering work on neutron crystallography and its application to biology.  Benno has published over 100 publications on the subject, and has mentored, trained and inspired numerous students, post-docs and early-career researchers, expanding the reach of neutron crystallography to a larger community of scientists and setting the grounds for its further development.

 

Benno graduated in physics from the University of New South Wales, Australia and completed his post-doctoral research at the University of California in San Francisco. From 1964 to 1966 he was a visiting scientist at the Cavendish Laboratory, at Cambridge University. Those were exciting times in the history of structural biology, and Cambridge was the place to be: John Kendrew and Max Perutz had in fact just received the Nobel Prize for solving for the first time the x-ray structure of two macromolecules, myoglobin and hemoglobin. However, neutron diffraction was still considered an unviable technique for macromolecular structural investigations. Benno was determined to change this view and set up to solving the three-dimensional structure of myoglobin using neutron crystallography. Shortly after leaving Cambridge, he joined the staff at Brookhaven National Laboratory, where he was able to record initial neutron diffraction data. His endeavors gave the long-yearned results in 1969, proving not only that the technique was feasible, but also that it could yield invaluable structural information on the position of hydrogen atoms, which are not visible with x-ray crystallography but are key players for the structural and functional integrity of proteins. Since his first structure, he applied neutron scattering to a large variety of biologically relevant molecules, such as the 30S subunit of the bacterial ribosome, ATPase, gramicidin A, thermolysin, hemoglobin, and the acetylcholine receptor. Being one of the pioneers of the technique, Benno put a lot of effort into optimizing the available instrumentation and neutron scattering facilities in the USA. With Paul Langan, he promoted the creation of the first neutron protein crystallography beamline in North America, the Protein Crystallography Station (PCS) at the pulsed neutron source at Los Alamos Neutron Science Center (LANSCE), a state-of-the-art facility that helps users in every step of a neutron diffraction experiment, from protein production and deuteration, to data collection and analysis.

 

The Bau Neutron Diffraction Award is given in memory of Professor Robert Bau, University of Southern California (1969-2008) and President of the American Crystallographic Association (2006). Professor Bau made major contributions to the development of the technique of single-crystal neutron diffraction and to its applications in chemical and biomacromolecular crystallography. The award consists of an honorarium and travel reimbursement to accept the award and deliver the award lecture at an ACA annual meeting. Schoenborn is the second recipient of this triennial award.

 

The award presentation and lecture is scheduled for Monday, July 25, at 8:00am.

 

 

2016 Etter Early Career Award to Jason Benedict

Jason Benedict, Assistant Professor of Chemistry at the University of Buffalo, is the recipient of the 2016 Margaret C. Etter Early Career Award. Established in 2002, the Etter Award recognizes the outstanding work of scientists who are in the early stages of their independent careers in the field of crystallography.

 

Jason received his Bachelor of Science in Chemistry in 2001 from Arizona State University, working in the field of fundamental reactions in inorganic chemistry. He completed his doctoral studies in 2007 at the University of Washington under the guidance of Bart Kahr, where he investigated the optical properties of oriented chromophores within technologically important materials. From 2008-2011, he was a postdoctoral fellow at the University of Buffalo in the laboratory of Prof. Philip Coppens.  His postdoctoral studies involved time-resolved x-ray diffraction experiments and the synthesis of novel polyoxotitanate clusters for use in solar energy applications. In 2011, Jason began his independent career as an Assistant Professor of Chemistry at the University of Buffalo. His current research efforts are aimed at developing an understanding at the molecular level of the physical processes that occur in stimuli-responsive nanoporous materials with the goal of creating "by design" crystalline materials with tailor-made properties.

During his independent career, Jason has made many outstanding contributions towards the development of new materials and advanced x-ray diffraction methods to characterize their properties. His group recently reported some of the first diarylethene-based photo-responsive metal-organic frameworks that exhibit unusual photoswitching and fatigue properties. Furthermore, he has pioneered new crystallographic methods such as an optical chopper that allows ultrafast x-ray diffraction measurements to be conducted using laboratory sources and an environmental cell that permits examination of the exchange of guest species incorporated within porous materials.

 

In addition to his stellar research accomplishments, Jason has been consistently recognized as an outstanding mentor to students at all levels. He recently received national attention for launching the US Crystal Growing Competition in 2014, which aims to teach the fundamentals of crystallography to students and educators in the K-12 level across the nation. While at the helm of the Western New York Undergraduate Research Symposium, this event that recognizes undergraduate research has grown to almost 100 participants from over 15 regional institutions. Dr. Benedict has also demonstrated a commitment to advancing diversity in the scientific community as exemplified within his own laboratory.

 

The award presentation and lecture is scheduled for Sunday, July 24, at 8:00am.