December 2011: Privé Lab

Dr. Gil Privé
Senior Scientist, Ontario Cancer Institute
Professor, University of Toronto
Department of Medical Biophysics
Department of Biochemistry

The Privé Lab is interested in protein structure, molecular recognition, transcriptional repression and membrane proteins. Most projects have the theme of understanding protein-protein, protein-peptide and protein-lipid interactions at the molecular level and relating this to function. They use biochemical and biophysical techniques, including X-ray crystallography.

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November 2011: P. John Hart

Professor P. John Hart 
Ewing Halsell - President's Council Distinguished Professor 
Department of Biochemistry 
UT Health Science Center 
San Antonio, TX, USA

Researchers in the Hart laboratory combine the use of single crystal X-ray diffraction with a wide range of molecular biological, biochemical, and biophysical methods to characterize macromolecules of fundamental biological and medicinal interest. An enumeration of current research topics and an indication of future research directions include: copper-zinc superoxide dismutase (SOD1) mechanistic studies, mutations in SOD1 and familial ALS, the copper chaperone for SOD1, mononuclear blue copper proteins of the phytocyanin class, targets for drug design in Mycobacterium tuberculosis, and targets for drug design from Francisella tularensis.

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October 2011: Prof. Stephen Curry

Imperial College London 
Biophysics Section 
Division of Cell and Molecular Biology 
Department of Life Sciences 
Faculty of Natural Sciences

Stephen Curry's group uses X-ray crystallography to see what the molecules of life look like and figure out how they work. Their main focus is on the molecular details of how certain RNA viruses cause infection and disease. For example, they work on cellular RNA-binding proteins such as PTB, La and Ebp1 that are press-ganged to help with viral translation. They also study viral enzymes, such as the 3C protease from foot-and-mouth diseases virus (FMDV).

Their investigations also encompass protein-drug interactions to try to understand what makes drugs stick to a particular protein target. Their work on human serum albumin (HSA), an abundant blood protein that binds and affects the action of many drugs, is helping to reveal the structural basis of its remarkably versatile binding capacity.

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September 2011: Prof. Dr. Oliver Einsle

Lehrstuhl für Biochemie
Institut für Organische Chemie und Biochemie
Albert-Ludwigs-Universität Freiburg

The Einsle lab is well staffed with Senior Scientist, Stefan Gerhardt, two postdoctoral fellows, ten doctoral students, and nine diploma students.

The goal of the Einsle group is to understand the functional properties of complex biochemical machines. This involves a broad range of methodologies ranging from microbiology and molecular biology and protein biochemistry to analytical tools such as EPR spectroscopy or isothermal titration calorimetry (ITC). Their key technique is the determination of three-dimensional structures by X-ray crystallography.

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Research Institutes in the Spotlight

July 2011: Kaspar P. Locher Lab

Kaspar P. Locher Lab 
Institute of Molecular Biology and Biophysics, ETH Zurich

Dr. Locher (Associate Professor of Molecular Membrane Biology) received his Ph.D. from the University of Basel in 1998. He now has a large group of 16 students and post-docs actively engaged in research.

Professor Locher's laboratory investigates the structures and mechanisms of various membrane proteins. Its main focus is on active transport proteins that catalyze processes such as nutrient uptake, drug extrusion, or lipid flipping. A more recent topic is the study of N-linked glycosylation, catalyzed by the membrane-integral oligosaccharyltransferase. The goal is to assemble molecular "movies" of these reactions by combining high-resolution structures of the proteins, obtained by X-ray crystallography, with biochemical and biophysical studies.

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June 2011: Wang Lab @ Academia Sinica

Andrew H.-J. Wang 
Distinguished Research Fellow and Vice President, Academia Sinica; Institute of Biological Chemistry, Academia Sinica 11 Post Docs, 9 Ph.D. students, 10 lab assistants, 29 alumni.

Structural proteomics, anticancer drugs, X-ray crystallography, NMR and molecular design.

Structural enzymology: Several enzymes as potential targets for drug discovery are under investigation. For developing new antibiotics, they focus on prenyltransferases and glyco-related enzymes. For anti-viral and anticancer agents, they analyze proteases (3CL proteases, MMPs), and phosphatases (DuSPs in signal transduction). Studies of potential targets for diabetics and Alzeheimer's disease are also in progress. Protein-anticancer drug-DNA interactions: Some DNA-binding proteins (like chromosomal proteins and proteins involved in meiosis) and many important anticancer drugs with DNA are of interest. The results can be useful for the design of new anticancer agents. Search for disease markers: Proteomic approaches, including 2D-GE and nanoLC, mass spectrometry and bioinformatics, are used to analyze cells and tissues from certain diseases to identify potential marker proteins. They are particularly interested in serum samples. Proteins from extreme environments: Microorganisms that live in extreme environments including extreme heat, cold, pH (acidic or alkaline) or radiation resistance have unusual proteins. Some enzymes described above are from those organisms.

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May 2011: Remaut Lab @ VIB

Ribbon representation of the PapC130-640 translocation channel viewed from the extracellular side. Remaut H, Tang C, Henderson NS, Pinkner JS, Wang T, Hultgren SJ, Thanassi DG, Waksman G, Li H. Cell. 2008 May 16;133(4):640-52.

Han Remaut
VIB Group Leader
VIB Laboratory of Structural and Molecular Microbiology Vrije Universiteit Brussel

Dr. Han Remaut's structural biology research lab is associated with VIB, a life sciences research institute, based in Flanders, Belgium. Scientists at VIB perform basic research with a strong focus on translating scientific results into pharmaceutical, agricultural and industrial applications.

Work in Remaut's group focuses on the structural molecular biology of bacterial cell surfaces and host-pathogen interactions. In an era of increased antibiotics resistance and difficulties in controlling hospital-acquired infections, Remaut's research is focused on gaining a better understanding of the fundamental principles governing the infection process. The lab studies the structural molecular biology of bacterial adhesins and cell-surface filaments with respect to their function in bacterial pathogenesis, with the ultimate aim of developing a new generation of virulence-targeted antimicrobials.

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April 2011: Garavito Lab @ MSU

R. Michael Garavito
Professor
Department of Biochemistry and Molecular Biology
Michigan State University

The focus of the Garavito laboratory is on the determination of the 3-dimensional structures of biological macromolecules by X-ray crystallography and the elucidation of their structure-function relationships. Of major interest are the structures of integral membrane proteins, enzymes involved in the biosynthesis of membrane components, and large macromolecular complexes that interact with biological membranes. Some of the former projects they have worked on include small peptide structures and E. coli outer membrane porins. In addition, they also have had a long-term research effort to develop methods for crystallizing membrane proteins.

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March  2011: Gouaux Lab @ HHMI

The Gouaux laboratory studies the molecular principles underpinning the structure and function of chemical synapses.

Eric Gouaux, Ph.D. is a senior scientist at the Oregon Health & Science University, Vollum Institute and Investigator at the Howard Hughes Medical Institute. The Vollum Institute is dedicated to basic research focusing on gene regulation, structural biology, cell signaling, molecular neuroscience and synaptic modulation with implications for human diseases ranging from autism and other neurodevelopmental disorders to Parkinson's disease, multiple sclerosis, psychiatric diseases and mechanisms of drug addiction.

Members of the Gouaux laboratory (16 members including postdocs, graduate students, and senior research associates) study the molecular principles underpinning the structure and function of chemical synapses. These specialized junctions are the primary sites of communication between neurons and are fundamental to the development and function of the peripheral and central nervous systems. Disruption of signal transduction at chemical synapses is implicated in a broad range of diseases, disorders and injuries and thus their studies not only provide fundamental insights into a crucial element of the nervous system but they also can be exploited for the development of new therapeutic agents.

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February  2011: Douglas C. Rees Lab @ CalTech

Douglas C. Rees Lab - A Howard Hughes Medical Institute Research Laboratory in the Division of Chemistry at the California Institute of Technology.

The research interests of the Rees group (a Howard Hughes Medical Institute Research Laboratory in the Division of Chemistry at the California Institute of Technology) emphasize the general area of structural bioenergetics, using crystallographic and functional ap­proaches to characterize water-soluble and membrane proteins participating in various energy transduction pathways. Studies of metalloproteins containing complex cofactors with either molybdenum or tungsten have defined the unusual structures of the FeMo-cofactor of nitrogenase and the more wide­spread Mo-cofactor that participate in basic reactions of the biological nitrogen and sulfur cycles. Studies of integral membrane proteins have emphasized energy transduction processes associated with photosynthetic and respiratory processes, mechanosensation, and of ABC transporter systems that mediate nutrient uptake into bacteria.

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January 2011: Stubbs Lab @ Martin Luther University of Halle – Wittenberg

The Stubbs Lab group

The main interests of Professor Milton Stubbs' lab lie in the field of "rational drug design," where they try to fuse the experimental structural data and thermodynamic measurements of protein ligand interactions in a computational framework to advance the drug discovery process. Structure deter­minations of various members of serine proteinases have provided a basis for computer-based drug design within this class of enzymes. In many proteins of interest, however, this course is blocked through a lack of suitable crystals. As a strategy for circumventing such problems, they are investigating the use of surrogate proteins for studying protein-ligand interactions. To test the feasibility of this approach, they have chosen bovine trypsin as a scaffold to reconstruct the ligand binding site of factor Xa.

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December 2010: Hao Wu Lab @ Cornell University

Hao Wu Group at the Department of Biochemistry, Weill Medical College of Cornell University.

Hao Wu's lab uses primarily X-ray crystallography in conjunction with other biophysical and biochemical methods to elucidate the protein-protein interactions involved in the intracellular signaling of cell survival and cell death in response to extracellular signals. The lab currently has nine postdoctoral fellows and four graduate students. A review of lab's alumni members showz that Hao Wu has populated the globe with faculty members and research scientists in academic and medical research facilities.

Hao Wu was editor of the book TNF Receptor Associated Factors (Advances in Experimental Medicine and Biology, volume 597), a seminal textbook in her field, and published the following recent paper: Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signaling. Su-Chang Lin, Yu-Chih Lo and Hao Wu. Nature (2010), 465: 885-90.

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November  2010: Jovine Lab @ Karolinska Institutet

From the Jovine Lab at the Karolinska Institutet: insights into egg coat assembly and egg-sperm interaction from the X-Ray structure of full-length ZP3 (Han et al., 2010).

Members of Dr. Luca Jovine's laboratory at the Karolinska Institutet (Department of Biosciences and Nutrition & Center for Biosciences, Huddinge, Sweden) study the molecular basis for the beginning of life. By marking the very beginning of a new individual, egg-sperm interaction at fertilization is a crucial step in the life cycle of all sexual organisms. Scanning electron microscopy pictures taken since the early 1960's have captured the collective imagination by offering low resolution glimpses of this event in humans. However, more than 40 years later, the molecular details underlying the species-specific embrace between mammalian germ cells remain obscure. The ultimate aim of their laboratory is to use structural biology to provide a definitive answer to this fundamental biological problem with important evolutionary implications.

Luca Jovine, Ph.D., group leader and EMBO young investigator has one postdoctoral fellow and three graduate students in his six-person group. Prof. Jovine did his doctoral work at the MRC Laboratory of Molecular Biology in Cambridge with subsequent postdoctoral studies at Mount Sinai School of Medicine in New York.

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October 2010: Gouaux Lab @ Oregon H&S University

From the Gouaux Lab at Oregon Health & Science University: the AMPA-sensitive GluA2 ionotropic glutamate receptor (Sobolevsky et al., 2009)

Members of Dr. Eric Gouaux's laboratory study the molecular principles underpinning the structure and function of chemical synapses. These specialized junctions are the primary sites of communication between neurons and are fundamental to the development and function of the peripheral and central nervous systems. Disruption of signal transduction at chemical synapses is implicated in a broad range of diseases, disorders and injuries and thus their studies not only provide fundamental insights into a crucial element of the nervous system but they also can be exploited for the development of new therapeutic agents.

Work includes studies of ionotropic glutamate receptors, ATP-gated P2X receptors and acid sensitive ion channels, as well as sodium-coupled glutamate, glycine, GABA and biogenic amine transporters. The group employs multiple biochemical, biophysical and electrophysiological methods to investigate the structure and biological functions of these molecules, with a particular emphasis on X-ray diffraction methods.

J. Eric Gouaux, Ph.D., senior scientist at the Vollum Institute and Howard Hughes Medical Institute Investigator, was elected to the National Academy of Sciences in 2010. As part of the NAS, Dr. Gouaux serves as scientific adviser to the U.S. government.

The Gouaux Lab currently has sixteen members, including 9 postdocs and 3 graduate students. If you are interested in joining the lab, please contact Prof. Gouaux at the address listed on the lab home page.

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September 2010: Waksman Lab @ Birkbeck College

From the Waksman lab at the Institute of Structural Molecular Biology, Birkbeck and University College London: structure of the translocator domain of the Hia trimeric autotransporter.

Gabriel Waksman's Labat the Institute of Structural Molecular Biology, Birkbeck and University College London is focused on gaining insight into the structural and molecular basis of secretion in Gram-negative bacterial pathogens. Dr. Waksman and his group of 8 postdocs and 3 graduate students are particularly interested in unraveling the structures of large, multicomponent assembly systems acting as nanopumps.

Specifically, work is focused on the structural biology of bacterial secretion systems, biophysical studies of SH2 domains, and structural and functional studies of DNA Polymerase I enzymes.

Credentials for Gabriel Waksman, PhD, FMedSci include:

• Courtauld Professor of Biochemistry at UCL
• Professor of Structural Molecular Biology at UCL and Birkbeck
• Wolfson - Royal Society Research Merit Award 2003 — EMBO Member 2007 — Academy of Medical Sciences 2008
• Director, Institute of Structural Molecular Biology
• Head, School of Crystallography, Birkbeck College
• Head, Department of Biochemistry and Molecular Biology,
  University College London.

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August 2010: Kuriyan Lab, UC Berkeley

Prof. John Kuriyan, Chancellor's Professor, Department of Molecular and Cell Biology & Department of Chemistry, University of California, Berkeley; Investigator, Howard Hughes Medical Institute.

John Kuriyan's Laboratory at UC Berkeley is interested in the structure and mechanism of the enzymes and molecular switches that carry out cellular signal transduction and DNA replication. They use X-ray crystallography to determine the three-dimensional structures of proteins involved in signaling and replication, as well as biochemical, biophysical, and computational analyses to figure out how they work. A major focus in their laboratory is understanding the allosteric mechanisms that enable proteins to be exquisitely sensitive to input signals

Cell Signaling: The major class of signaling molecules that they study are the protein kinases, a large family of closely related enzymes that catalyze the addition of phosphate to serine, threonine, and tyrosine residues in proteins.

Processive DNA Replication: DNA polymerases that replicate chromosomes achieve high speed by utilizing specialized proteins that allow the polymerase to move rapidly along DNA without letting go. These proteins include the "sliding DNA clamp" and the clamp loader complex that couples ATP binding and hydrolysis to the opening of the beta clamp and its loading onto DNA.

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July 2010: UT Southwestern Medical Center

As one of the world's foremost research institutions, UT Southwestern Medical Center (UTSWMC) is leading the way in a new era of scientific discovery in the 21st century. Their biomedical research has yielded dramatic discoveries that hold great promise for understanding the nature of human disease. For basic or clinical research, UT Southwestern — an institution that fosters multidisciplinary approaches and rigorous scientific training — provides an ideal research environment.

UTSWMC focuses on attracting and retaining pre-eminent researchers, while maintaining a culture environment that promotes research in diverse areas. They have four Nobel Laureates (pictured above: Alfred Gilman, Joseph L. Goldstein, Johann Deisenhofer, Michael S. Brown, three of whom are active faculty members), 18 members of the National Academy of Sciences, and 18 members of its Institute of Medicine (as of June 2009). UTSWMC also has more than 3,500 research projects under way with more than $400 million in annual funding.

UT Southwestern Medical Center is distinguished by the quality of its biomedical research, which consistently ranks among the best in the world. Shanghai Jiao Tong's Academic Ranking of World Universities places UTSWMC 6th in the world for the impact and quality of research in the Life Sciences. Thomson Science Watch ranks UTSWMC 7th for the average quality of its research as measured by citations per paper.

Members of the structural biology department who are involved in protein crystallograpy include: Johann Deisenhofer, Kevin Gardner, Elizabeth Goldsmith, Youxing Jiang, Zbyszek Otwinowski, Rama Ranganathan, Jose Rizo-Rey (Josep Rizo), Michael Rosen, Diana Tomchick and Hong Zhang.

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June 2010: Biotechnology Program at Texas Tech University and Department of Cell Physiology and Molecular Biophysics at Texas Tech University Health Sciences Center

Prof. Bryan Sutton has organized a unique course, for the Biotechnology Program at Texas Tech University and Department of Cell Physiology and Molecular Biophysics at Texas Tech University Health Sciences Center, to introduce students of all types to some of the principles of structural biology. The fundamental concept of this course is to involve students in real-life science, while still learning some of the basic concepts of protein structure and structural biology. The course is entitled, Deep Saturation Mutagenesis (DSM); a concept borrowed from the Hubble Telescope Deep Field (HDF) project.

In the HDF, a very small region of the sky was exposed to the Hubble Telescope's cameras for a period of 10 days. The resulting image was a highly detailed view of deep space. DSM utilizes similar ideas, but for protein structure. Over the lifetime of the course, they will introduce all possible point mutations at all locations in a single enzyme, and measure the resulting effects on enzymatic activity and protein structure. Similar saturation type mutagenesis has been attempted for other proteins, but not to this degree.

Their target protein is glutaredoxin from Synechocystis sp., as this small enzyme possesses only 89 amino acids; further, related proteins are already well characterized from a crystallographic perspective. At the beginning of the course, the students will select a single point mutation, at random; there are 1690 possible point mutations required to achieve complete saturation of this protein.

The students will learn mutagenesis, protein purification and protein crystallization. They will then collect their X-ray data on the Rigaku ScreenMachine located at TTUHSC. After solving the X-ray structure, and learning some basic X-ray refinement principles, students will learn how to interpret their results. Of course, all mutations will not be tractable; however, they consider that valid data.

All of the data obtained over the lifetime of the course will be maintained by a Laboratory Information Management System (LIMS), so the students will also become familiar with a more rigorous style of data management. This course is intended to become viral; and, thus they will eventually make this course available to other Universities and Colleges. Prof. Sutton would also like to conduct abbreviated summer sessions, where High School science teachers could learn up-to-date biochemical techniques and contribute to the distributed effort of this experiment.

Their DSM course is not intended to train professional protein X-ray crystallographers. However, with the advent of newer technologies such as the ScreenMachine, it is intended to introduce students from a wide-variety of backgrounds to principles to which they would not normally be exposed.

Professor Sutton's research interest is in the biophysics of C2 domains. C2 domains are membrane interacting domains that are common to a wide-range of proteins. His group's present focus is on the C2 domains of synaptotagmin and the C2 domains of human dysferlin. Synaptotagmin is the major Ca²⁺ sensor in neuron and mutations in dysferlin have been implicated in Limb-Girdle muscular dystrophy in humans.

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May 2010: University of British Columbia, Dept. of Biochemistry and Molecular Biology

For more than fifty years the UBC Department of Biochemistry & Molecular Biology has played an active and important role at UBC and in the greater scientific community. The Department includes 27 full-time faculty, some of whom are affiliated with research groups such as the BC Cancer Agency or the Centre for Blood Research. The department also has eleven associate faculty members.

Since its move to the new multidisciplinary Life Sciences Centre, the department has been brought together with the departments of Cellular & Physiological Sciences and Microbiology & Immunology, as well as independent researchers from Medical Genetics and Zoology. By working with members of other departments in this highly interactive environment, the UBC Department of Biochemistry & Molecular Biology continues to grow and develop in its role as one of the leaders in the field. Three of the faculty are X-ray crystallographers involved in structural biology.

The current research effort in Prof. Gary Brayer's group is focused on two proteins: the first involves the critical digestive enzyme human pancreatic alpha-amylase while the second system involves a unique hexameric form of the enzyme citrate synthase, which is only found in Gram-negative bacteria.

Professor Natalie Strynadka has, as a research goal, the structure-based design of novel, therapeutically useful antibiotics and inhibitors of antibiotic-resistance mechanisms. To achieve this goal, her group employs a combination of X-ray crystallography, molecular modelling, molecular docking and molecular biology in collaboration with medicinal chemistry to engineer drugs that specifically interact with and disable critical bacterial target proteins.

Assistant Professor Filip Van Petegem is engaged in research on ion channels that allow the selective passage of Ca²⁺, how they interact with regulatory proteins, how they integrate various signals, and what their molecular architecture looks like. In particular, his group is investigating two classes of channels: voltage-gated calcium channels (CaVs) and ryanodine receptors (RyRs).

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April 2010: Indiana University School of Medicine, Dept. of Biochemistry and Molecular Biology

The Department of Biochemistry and Molecular Biology at Indiana University School of Medicine is in the midst of a vigorous expansion phase. They have had 9 new faculty members join the department during the past three years and currently have plans to hire 4-6 additional faculty over the next few years. The Department currently has 24 primary faculty members engaged in research and teaching with a focus on understanding the biochemical and molecular basis of fundamentally important life processes.

Prof. Thomas D. Hurley's area of study involves X-ray crystallography of dehydrogenases, enzyme engineering using site-directed mutagenesis as well as kinetic and thermodynamic analysis of protein ligand interactions.

Eight faculty members comprise the structural biology section of the Department. Chancellor's Professor and Associate Chairman Thomas D. Hurley serves as the Director of Center for Structural Biology and has - as a major focus of his research - to understand, at the molecular level, the processes involved in the recognition and binding of substrates to enzyme active sites. Associate Professor Millie M. Georgiadis serves as Graduate Admissions Chairman and has a research focus that includes X-ray crystallographic, biochemical, and thermodynamic studies of protein-nucleic acid interactions involved in replication, nuclear export, and temporal gene expression. Assistant Professor Quyen Hoang's group works on the structural biology of neurodegenerative disease and structure-based drug design. The research in Assistant Professor Yuichiro Takagi's laboratory focuses on biochemical and structural analysis of the multi-protein complexes that control gene regulation in eukaryotes. Associate Professor Qi-Zhuang Ye's research currently focuses on studying structure and function of methionine aminopeptidases (MetAPs).

Interests of Prof. William F. Bosron include the structure and mechanism of alcohol dehydrogenases and carboxylesterases, regulation of ethanol, as well as retinoid and drug ester metabolism. Molecular design of small molecules and proteins to modulate cellular processes in cancer is the focus of Assistant Professor Samy Meroueh. Finally, Chairman of the Department, Professor Zhong-Yin Zhang is active in researching the signaling mediated by tyrosine dephosphorylation and targeting protein tyrosine phosphatases for the treatment of cancer, diabetes/obesity, autoimmune disorders, and infectious diseases.

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February 2010: ESFRI-INSTRUCT - Core Center G

Within the Department of Molecular Membrane Biology at the Max-Planck-Institut für Biophysik in Frankfurt resides the ESFRI-INSTRUCT - Core Center G. Upgrading and expanding the X-ray crystallography facility at the Max-Planck Institute of Biophysics was part of a recent initiative by ESFRI-INSTRUCT (European Strategy Forum on Research Infrastructures - Integrated Structural Biology Infrastructure) to elevate the Max-Planck Institute of Biophysics to be one of the seven core European centers for structural biology.

Prof. Dr. Dr. h.c. Hartmut Michel, winner of Nobel Prize for Chemistry in 1988, leads the Department of Molecular Membrane Biology which oversees Core Center G. For the preparatory phase, the BMBF (German Ministry of Education and Research) has funded the effort, with the majority of the funds being invested to improve the X-ray crystallographic equipment managed by Dr. Juergen Koepke. The center now includes two Rigaku rotating anode based crystallography systems (MicroMax-007 HF and a FR-E+ SuperBright X-ray sources) and a CrystalMation automated crystallization system tended by Dr. Yvonne Thielmann.

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January 2010: Yigong Shi @ Tsinghua University

A leading Chinese researcher in the field of protein X-ray crystallography, Dr. Shi has determined the crystal structure of several critical apoptotic proteins, including apaf-1, DIAP1, and the BIR3 domain of XIAP. He began his independent career as an Assistant professor in the Department of Molecular Biology at Princeton University in 1998. He was promoted to the ranks of Associate Professor in 2001 and Professor in 2003. At an age of 36, he became the youngest, tenured Full Professor in the history of Princeton's Department of Molecular Biology (Warner-Lambert/Parke-Davis Professor). In June 2008, he was selected as a Howard Hughes Medical Institute investigator but instead resigned his position at Princeton University in order to pursue a career at Tsinghua University. This was in response to an effort to repatriate Chinese scientists.

Scientific research in Dr. Shi's laboratory is aimed at understanding the structural and molecular mechanisms involved in tumorigenesis, with a focus on key regulatory components in the apoptotic pathways and other important cellular processes. He has published over 90 papers in international journals, including as corresponding author eleven in Cell, six in Nature, and three in Science. Dr. Shi was awarded the Irving Sigal Young Investigator Award by the Protein Society in 2003 and became the first Chinese scientist to win such honor. He has been the President of the Chinese Biological Investigators Society (CBIS) since 2005.

Dr. Shi was appointed a Chair Professor of Tsinghua's Department of Biological Sciences and Biotechnology in 2003 and a Tsinghua Changjiang Professor in 2006. He becomes Vice Director of Tsinghua's Institute of Biomedicine and Vice Dean of Tsinghua's Department of Biological Sciences and Biotechnology in 2007.

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