Australia (planned)

• Structural genomics of microbial virulence factors (planned)
  P.Is. : Jamie Rossjohn, and James Whisstock, Monash University, Melbourne
  
  
• Focused structural genomics of macrophage protein (planned)
  P.Is. : Bostjan Kobe, Jenny Martin, David Hume, and Thomas Huber, Univ. Queensland, Brisbane
  
  
• Structural genomics of cold-adapted organisms (planned)
  P.Is. : Paul Curmi, and Rick Cavicchioli, University of New South Wales, Sydney

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Canada

• Ontario Centre for Structural Proteomics
  P.Is. : Cheryl Arrowsmith, and Aled Edwards, Univ. Toronto
  
  Description: The initiative started with a main focus of genome-scale structural biology with the goal of deducing functions from structures. Thermophilic archaea, Methanobacterium thermoautotrophicum,Helicobactor pylori, and other bacterial, eukaryote, and archeal proteins are selected as targeted organisms. Project's strong focus has been on a large-scale sample preparation and purification in addition to the structural determination by X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy.
  
  
• Montreal-Kingston Bacterial Structural Genomics Initiative
  P.I. : Mirek Cygler
  
  Description: A pilot project of bacterial structural genomics was undertaken in 2000. The emphasis of this project is on providing structural representatives for protein families rather than to concentrate on a specific organism. The project's selection criteria for protein families serves three objectives; 1) lead to understand the enzymes, 2) determine structures with unknown molecular functions, 3) provide structural framework for development of antibacterial agents by selecting targets from the identified essential genes or from the ORFs common to several pathogens.
  
  Supported by: National Research Council of Canada, the Canadian Institutes of Health Research
  
  
• Montreal Network for Pharmaco-Proteomics and Structural Genomics
  P.I. : Mirek Cygler
  
  Description: The aim of this project is to set up a facility to allow researchers to investigate the function and structure of genes and proteins that can be used in developing new drugs. The facility will emphasize protein mapping, identification and characterization. One project, the cell map, involves mapping and characterizing proteins and how they are associated with all parts of a cell. Another project, molecular machines, involves using assays to map and validate protein interactions with other proteins, and the third, structural genomics, analyzes the structures of key proteins. The project will bring together investigators who use biochemical, cell biological, genomics, engineering, DNA chip technology, protein sequence analysis, and X-ray crystallography, among other innovative disciplines and technologies.
  
  Supported by: Genome Quebec/Genome Canada
  
  
• CyberCell project
  P.I. : Michael Ellison (structure/ function team)
  
  Description: The CyberCell project aims to simulate the Escherichia coli cell for understanding the living systems. Structure/ Function team of the CyberCell plans to understand proteins that are either essential or important to E. coli growth and viability under defined conditions. The project determines the E. coli structural proteins by X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy and expects a throughput of 45 structure determinations per year.

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EU

• Structural Proteomics in Europe (SPINE) - European Commission fifth Framework program (FP5) "QLG2-CT-2002-00988"-
  P.Is. : Stephen Cusack, EMBL, France, Robert Kaptein, Utrecht Univ., the Netherlands, Dino Moras, CNRS, France, David Stuart, University of Oxford, UK, and Joel Sussman, Weizmann Institute of Science, Israel and Keith Wilson, University of York, UK. (Coordinated at the Division of Structural Biology, University of Oxford)
  
  Description: SPINE targets the structures of a set of human proteins implicated in disease states, in particular, cancer, and neurodegenerative diseases, together with proteins from a set of pathogenic viruses and bacteria, including Herpes viruses and Mycobacterial tuberculosis. It is planned that around 30 bacterial and 30 human/viral structures will be determined in the first year, rising to around 300 of each by the end of Year 3. Both nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography are used for structural determination.
  
  Supported by: European Union
  
  
• -European Commission sixth Framework program (FP6)- (planned)

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France

• Structural Genomics of Mycobacteria
  P.Is. : Stewart Cole,and Pedro Alzari, Institut Pasteur
  Associated partner : Christian Cambillau & Yves Bourne (Marseilles,France)
  
  Description: Mycobacterium tuberculosis, M. leprae, and M. bovis are the target organisms envisioning for new antibacterial agents discovery. Building upon the achievements of mycobacterial genomics at the Pasteur Institute, this structural genomics project focuses mainly on mycobacterial proteins of unknown function, with the explicit aim of identifying new targets for drug and vaccine discovery. The project is part of two European-funded consortia: "Structural and Functional Genomics of Mycobacterium tuberculosis" (X-TB) and "Structural proteomics in Europe" (SPINE).
  
  Supported by: the Pasteur Institute, the Genopole Programme, the Ministry of Research and the European Union.
  
  
  
  
• Structural Genomics of Eukaroytes
  P.I. : Dino Moras, IGBMC
  • IGBMC Illkirch, EMBL Grenoble, Univ. Montpellier etc.
  
  Description: The project plans to research on the nuclear hormone receptor, using X-ray crystallographic technique. It is a part of the European Union (EU) funded consortium called Structural Proteomics in Europe (SPINE).
  
  Supported by: The Strasbourg Alsace-Lorraine Genopole and the Grand-Est Cancéropole and the European SPINE network
  
  
• Yeast Structural Genomics
  P.I. : Joel Janin,and Herman Vantilbeurgh, Centre National de la Recherche Scientifique, Gif-sur-Yvette and Universite Paris-Sud, Orsay
  
  Description: The initiative involves expressing genomic ORFs in a systematic manner, purifying the proteins and determining their three-dimensional structures by X-ray crystallography and high-field nuclear magnetic resonance (NMR) spectroscopy. The first step is a three-year pilot project aiming to develop the technology for the efficient protein production and structure determination of about 20 proteins from the yeast Saccharomyces cerevisiae. The second step involves the creation of the Centre des Biostructures with the capacity to express and purify more than 1000 proteins from prokaryotic and eukaryotic genomes, and to determine several hundred three-dimensional structures every year. The initiative is a part of the European Union (EU) funded consortium called Structural Proteomics in Europe (SPINE).
  
  Supported by: the Genopole Programme of the Ministry of Research
  
  
• Marseilles Structural Genomics
  P.I. : Christian Cambillau, CNRS
  
  Description: The project is conducted by CNRS and industrial joint consortium aiming at the discovery of new anti-bacterial targets. The target proteins of this project are bacterial proteins (Escherichia coli and Mycobacterium tuberculosis) and viral proteins. Technologies of automation for large-scale protein production in E. coli using the Gateway^TM system and crystallization are being developed. For structural determination, X-ray crystallography is used.
  
  Supported by: the French Ministry of Industry, the French Ministry of Research and the European Union.
  

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Germany

• Protein Structure Factory
  P.I. : Udo Heinemann, Max-Delbr歡k-Centrum fur Molekulare Medizin, Berlin
  
  Description: Protein Structure Factory (PSF) is a collaborative project of the German Human Genome Project (DHGP) and structural biologists from the Berlin area. PSF is established to characterize human proteins encoded by the genes or cDNAs available at the Berlin Resource Center of DHGP. Target proteins are selected on grounds of predicted novelty of the structure as well as medical or biological relevance. PSF takes the protein expression method in Escherichia coli and Saccharomyces cerevisiae or Pichia pastoris and determines the three dimensional protein structures by nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography. Determination of 100-200 proteins per year are planned.
  
  
• German Federal Structural Genomics Project in Hamburg (planned)

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Israel

• The Israel Structural Proteomics Center (ISPC)
  P.Is. : Joel L. Sussman & Yigal Burstein, Gideon Schreiber and Israel Silman, Weizmann Institute of Science
  
  Description: The Israel Structural Proteomics Center (ISPC) was established by scientists from the Weizmann Institute of Science, Rehovot, ISRAEL to increase the efficiency of all stages of 3D protein structure determination. Targets submitted to the ISPC, are primarily related to human health and disease. The center has a unique combination of scientific expertise and state-of-the-art instrumentation for high-throughput production and crystallization of proteins. Each target is cloned into multiple vectors, using ligation independent cloning. Expression is extensively screened in several bacterial strains with different fusion proteins. Proteins, which are not soluble, are expressed either in bacterial cell free extracts or in yeast (Pichia pastoris). Parallel purification of up to 6 proteins can be performed using an AKTA3D. Purified proteins are screened for crystallization using a Douglas Instruments ORYX6 robot, which employs the batch method under oil. This has yielded a high-percentage of high quality diffracting crystals. All the different stages are manipulated by our laboratory information management system (LIMS) in which several bioinformatics tools have been incorporated to facilitate the analysis of our targets. The ISPC now receives targets from scientist both in academia and industry. We believe that making structural information accessible to the entire scientific community will stimulate novel studies and developments related to health and disease.
  
  Supported by: The Israel Ministry of Science and Technology, by the European Commission as one of the principal nodes in the Structural Proteomics in Europe (SPINE) project and by the Divadol Foundation.
  
  Contact information:
  Email: ISPC@weizmann.ac.il
  
  
  

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Japan

National Project on Protein Structural and Functional Analyses ("NPPSFA")



• Program for comprehensive studies, "NPPSFA"
  RIKEN Structural Genomics/Proteomics Initiative
  P.I. : Shigeyuki Yokoyama, RIKEN Genomic Sciences Center, and Harima Institute at SPring-8
  
  Description: RIKEN started the structural genomics/proteomics project as early as 1997. RSGI is conducted by a collaborative work by the RIKEN Genomic Sciences Center and Harima Institute at SPring-8. RSGI is now integrated into the Japanese national project, National Project on Protein Structural and Functional Analyses, which has started fiscal 2002 to study both structures and functions of proteins in selected biological systems. RSGI has two main components. One is genome-driven structural genomics to analyze the structures and functions of proteins encoded by the genome of an organism; a eubacterial extreme thermophile, Thermus thermophilus HB8 and an archaeal hyperthermophile, Pyrococcus horikoshii OT3. The other is to study structures and functions of medically/biologically important proteins from higher eukaryotes; human, mouse, and Arabidopsis thaliana in collaboration with pharmaceutical and chemical companies. For protein sample preparation, the cell-free protein synthesis method is routinely used in addition to authentic recombinant methods. Both X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy are used for structure determination.
  
  Supported by: Ministry of Education, Culture, Sports, Science and Technology (MEXT)
  
  
  
• Eight programs for focused studies, "NPPSFA"
  • Development and differentiation of organisms and replication and repair of DNA
    
    Structural Genomics Consortium for Research on Development and Differentiation of Organisms and Replication and Repair of DNA
    P.I. : Masaru Tanokura, Graduate School of Agricultural and Life Sciences, University of Tokyo
    
    Description: Japanese national project on structural genomics where university community takes a leading part has been established in fiscal 2002 under the name of "National Project on Protein Structural and Functional Analyses." The aim of this project is to study both structures and functions of proteins in a selected target of biological systems. In our consortium of this project, we will elucidate the structure and function of the proteins that are related to the development and differentiation of organisms and the replication and repair of DNA in order to display their intrinsic biological functions. The organizations comprising our consortium are: University of Tokyo, Chiba University, Ehime University, Fujita Health University, Gunma University, Kyushu University, Marine Biotechnology Institute, Mitsubishi Kagaku Institute of Life Sciences(MITILS), Nippon Medical School, Takara Bio Inc., Tokyo Institute of Technology, Tokyo Metropolitan University, and Tokyo University of Pharmacy and Life Science.
    
    Supported by: Ministry of Education, Culture, Sports, Science and Technology (MEXT)
    
    
  • Transcription and translation (gene expression system)
    
    
    Structural genomics consortium for research on gene expression system
    P.I. : Isao Tanaka, Graduate School of Science, Hokkaido University
    
    Description: Japanese national project on structural genomics where university community takes a leading part has been established in fiscal 2002 under the name of "National Project on Protein Structural and Functional Analyses." The aim of this project is to study both structures and functions of proteins in a selected target of biological systems. In this project, our consortium is organized to elucidate the structures and functions of the proteins that are involved in the protein synthesis at various stages (transcription, mRNA modification and transport, translation, and protein modification) for a better understanding of the gene expression system. Disorder in gene expression system causes various illness such as metabolic disease or autoimmune disease represented by congentinal disease, cancer, and diabetes mellitus. Thus, understanding of the gene expression system contributes not only to the development of the life science but also to the progress of the practical disease therapy. The organizations comprising the consortium are: Hokkaido University, Tohoku University, Shinshu University, The University of Tokyo, Institute of Medical Science, Ochanomizu University, Osaka University, Kyushu University, Kumamoto University, National Institute of Genetics, Nippon Institute for Biological Science, and National Institute of Advanced Industrial Science and Technology.
    
    Supported by: Ministry of Education, Culture, Sports, Science and Technology (MEXT)
    
    
    Structural Genomics Consortium for Research on transcription and translation
    P.I. : Yoshifumi Nishimura, Yokohama City Univ.
    
    Supported by: Ministry of Education, Culture, Sports, Science and Technology (MEXT)
    
    
  • Posttranslational modification and transport
    P.I. : Soichi Wakatsuki, High Energy Accelerator Research Org.
    
    Supported by: Ministry of Education, Culture, Sports, Science and Technology (MEXT)
    
    
  • Protein higher-order structure formation
    
    Structural Genomics Consortium for Research on Protein Higher-Order Structure Formation System
    P.I. : Kunio Miki, Graduate School of Science, Kyoto University
    
    Description: Japanese national project on structural genomics where Japanese university community takes a leading part has established in fiscal 2002 under the name of "National Project on Protein Structural and Functional Analyses." The aim of this project is to study both structures and functions of proteins in a selected target of biological systems. In our consortium of this project, we will elucidate the structures and functions of the proteins that are related to the higher-order structure formation of proteins in order to display their intrinsic biological functions, including molecular chaperon for protein folding, transfer of proteins across the membrane, the quality control of proteins by repair, recycling and degradation, and so on. The organizations comprising our consortium are: Kyoto University, Osaka University, Himeji Institute of Technology, Kyushu University, Toyama Medical and Pharmaceutical University, The University of Tokyo, Tokyo Institute of Technology, Tokyo University of Agriculture and Technology, and Kirin Brewery Co., Ltd.
    
    Supported by: Ministry of Education, Culture, Sports, Science and Technology (MEXT)
    
    
  • Intracellular Signal Transduction
    P.I. : Fuyuhiko Inagaki, Hokkaido Univ.
    
    Supported by: Ministry of Education, Culture, Sports, Science and Technology (MEXT)
    
    
  • Brain and nervous system
    
    Structural and Functional Proteomics Consortium for Research on the Proteins Working in Brain and Nervous System
    P.I. : Atsushi Nakagawa, Institute for Protein Research, Osaka University
    
    Description: Japanese national project on structural genomics where university community takes a leading part has been established in fiscal 2002 under the name of "National Project on Protein Structural and Functional Analyses." The aim of this project is to study both structures and functions of proteins in a selected target of biological systems. In our consortium of this project, we will elucidate the structure and function of the proteins that play key roles in brain and nervous system. The organizations comprising our consortium are: Osaka University, Ehime University, Himeji Institute of Technology, Hiroshima University, Kwansei Gakuin University, Nagoya University, Nara Institute of Science and Technology, Okayama University, Tokushima University, and the University of Tokyo. X-ray crystallography, NMR spectroscopy, bioinformatics, mass-spectroscopy, and other techniques are used to perform this project.
    
    Supported by: Ministry of Education, Culture, Sports, Science and Technology (MEXT)
    
    
  • Metabolic system
    
    Target Proteins: Metabolic System of Extremophiles
    P.I. : Seiki Kuramitsu, and sub P.I. : Ryoji Masui, Graduate School of Science, Osaka University
    
    Description: To understand the metabolic pathways and their regulation at a molecular level from the viewpoint of unity and diversity of organisms, this program aims to analyze proteins involved in biosynthesis and degradation of various cellular components, including proteins, nucleic acids and polysaccharides, and energy metabolism (photosynthesis, chemical synthesis, electron transport system, oxidative phosphorylation, etc.). The protein targets selected are from metabolic systems of extremophiles. The main organisms are archaeal aerobic hyperthermophiles, Sulfolobus tokodaii and Aeropyrum pernix. The other organisms are psycophiles and disease related microorganisms.
    
    Supported by: Ministry of Education, Culture, Sports, Science and Technology (MEXT)
  
  
  
  
• Biological Information Research Center (BIRC)

P.I. : Yoshimasa Kyogoku, Biological Information Research Center

Description: BIRC's project is composed of three main components; structural analysis of membrane proteins, functional analysis of human full-length cDNA, and construction of integrated biodatabase. Several techniques for structural determination, and functional analysis, and others will be developed. The project main target, membrane protein is hoped to lead to the drug discovery.

Supported by: Ministry of Economy, Trade and Industry

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Korea

• The Korean Structural Proteomics Research Organization

P.I. : Se Won Suh, Seoul National University

Description: The Korean Structural Proteomics Research Organization was established in February 2002 to promote and coordinate research activities in Korea. The major focus is on proteins such as Mycobacterium tuberculosis and Helicobacter pylori leading to drug discovery. X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy are used for structural determination.

Supported by: Korean Ministry of Science and Technology

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Switzerland

• National Center of Competence in Research (NCCR)

P.Is. : K. Wuethrich, T.J. Richmond, R. Glockshuber, N. Ban, F. Allain and W. van Gunsteren at the ETH Zurich, M. Gruetter, A. Plueckthun and A. Caflisch at the University of Zurich as well as F. Winkler at the Paul Scherrer Institute, Villigen and A. Engel at the University of Basel.

Description: The Swiss National Center of Competence in Research (NCCR) is a network of Swiss research groups working in the field of structural biology, which is in operation since May 2001. The research of this network encompasses the fields of recombinant protein technologies, macromolecular structure determination and computational biomolecular sciences applied to membrane proteins, supramolecular assemblies and molecular interactions.

Supported by: Swiss National Science Foundation, University of Zurich and ETH Zurich

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UK

• North West Structural Genomics Centre

P.Is. : Samar Hasnain, and John Helliwell, Daresbury Laboratory

Description: The ultimate aim of this project is to improve the understanding of host pathogen interactions, leading to the development of more effective drugs for human health and pathogen biology. Structure determination of at least 100+ proteins of direct importance to pathogen biology and human health is planned. The North West Structural Genomics Centre (NWSGC) will exploit the strengths of research groups from several North West Universities (Univ. Liverpool, Univ. Manchester, Univ. Leeds, Liverpool John Moores Univ., and Univ. of Manchester Inst. of Science and Technology), a major pharmaceutical company (AstraZeneca) and Daresbury Laboratory; as well as the unique resource offered by the close proximity to the UK Synchrotron Radiation Source. NWSGC is building a new Multipole Wiggler MAD Beamline at Daresbury Laboratory and a Protein Production Factory for the structure determination of proteins from pathogens including M. tuberculosis, plant pathogens, and Streptomyces. For high-throughput structural determination by X-ray Crystallography, technologies such as semi-automatic expression and purification system for soluble proteins will be developed.

Supported by: Biotechnology and Biological Sciences Research Council (BBSRC), Council for the Central Laboratory of the Research Councils (CLRC), The Engineering and Physical Sciences Research Council (EPSRC), Medical Research Council (MRC) etc.

poster presentation file at ICSG2002 by courtesy of Samar Hasnain
PowerPoint 6.2M



• Oxford Protein Production Facility

P.I. : David Stuart, University of Oxford

Description: The project mainly focuses the high-throughput protein expression, purification and crystallization of human and viral proteins with a focus that includes infection, immunology and cancer. Targets include proteins from herpes viruses, proteins involved in immune cell function, Zn fingers and transcription factors, protein-DNA complexes, and human proteins involved with cancer. Oxford Protein Production Facility (OPPF) plans to express proteins in bacteria, insect and mammalian cells and itﾕs goal is to process 1000 clones/year. The effort is part of a larger consortium that includes synchrotron beamlines. In addition to X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, cryo-electron microscopy will also be used for structural studies. OPPF is a part of the European Union (EU) funded consortium called Structural Proteomics in Europe (SPINE).

Supported by: University of Oxford, Medical Research Council, Cancer Research UK, Biotechnology and Biological Science Research Council (BBSRC), Welcome Trust, EU


• Cambridge Group
P.I. : Ernest Laue, University of Cambridge

Description: The groupﾕs main focus is protein-protein interactions that are important in cellular control. The project is composed of three projects; chromatin mediated transcriptional repression, cyclin-dependent kinases, and small G proteins involved in cellular control. Structural determination is mainly done by nuclear magnetic resonance (NMR) spectroscopy.

Supported by: University of Cambridge, Welcome Trust, Biotechnology and Biological Science Research Council (BBSRC), and European Union

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USA

• New York Structural Genomics Research Consortium

P.Is. : Stephen Burley, Structural GenomiX, and Jeffrey Bonanno, Rockefeller Univ.

Description: The consortium expects to solve several hundred of protein structures from humans and model organisms ranging from bacteria to humans with an emphasis to lead to the drug discovery. The consortium also focuses on developing key high-throughput technologies such as computing methods of protein family classification and target selection, protein production, purification, and structure determination by X-ray crystallography. The long-term goal of the NYSGRC is to determine the 10,000 plus three-dimensional protein structures.

Supported by: National Institute of General Medical Sciences (NIGMS)/ National Institute of Health (NIH) , National Center for Research Resources (NCRR)/ NIH, Department of Energy (DOE), and Howard Hughes Medical Institute (HHMI)


• Midwest Center for Structural Genomics

P.I. : Andrzej Joachimiak, Argonne Natl. Lab.

Description: The group will select protein targets from Eukarya, Archaea, and Bacteria, with an emphasis on previously unknown folds and on proteins from disease-causing organisms. Another concentration of this group is to set up methods for highly cost effective protein production, crystallization, structural determination by X-ray crystallography, and refinement with an estimate to reduce the average cost from $100,000 to $20,000.

Supported by: National Institute of GeneralMedical Sciences (NIGMS)/ National Institute of Health (NIH) and Department of Energy (DOE)


• Berkeley Structural Genomics Center

P.I. : Sung-Hou Kim, Lawrence Berkeley Natl. Lab.

Description: The main focus of this initiative is on integrated structural genomics effort of minimal organisms, Mycoplasma genitalium and Mycoplasma pneumoniae to study proteins essential for life. The goals are classifying fold families, obtaining representative proteins from each family, inferring molecular functions of proteins with no known function, and optimizing key steps for structure determination. Structures are determined by X-ray crystallography.

Supported by: National Institute of General Medical Sciences (NIGMS)/ National Institute of Health (NIH) and Department of Energy (DOE)


• Northeast Structural Genomics Consortium

P.I. : Gaetano Montelione, Rutgers Univ.

Description: The Northeast Structural Genomics Consortium (NESG) targets proteins from eukaryotic model organisms which are subjects of extensive functional genomics research, including S. cerevisiae, C. elegans, and D. melanogaster, as well as homologues from the human genome. NESG is to develop integrated key technologies such as protein expression and structural determination by both X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy. By developing high-throughput and cost effective platforms, NESG plans to have over 180 protein structures per year at a cost excluding capital equipment of $10,000 - $20,000 per structure.

Supported by: National Institute of General Medical Sciences (NIGMS)/ National Institute of Health (NIH)


• TB Structural Genomics Consortium

P.I. : Thomas Terwilliger, Los Alamos Natl. Lab.

Description: The consortium plans to determine and analyze the structures of over 400 proteins from Mycobacterium tuberculosis including about 40 novel folds and 200 representatives of new protein families and analyze in the context of functional information. This will be strongly directed to the design of new and improved drugs and vaccines for tuberculosis. High-throughput methodology developments have also been carried out as a pilot project using hyperthermophile. The consortium uses X-ray crystallography for structural determinations.

Supported by: National Institute of General Medical Sciences (NIGMS)/ National Institute of Health (NIH), National Institute of Allergy and Infectious Diseases (NIAID)/ NIH, and Department of Energy (DOE)


• Southeast Collaboratory for Structural Genomics

P.I. : Bi-Cheng Wang, Univ. of Georgia

Description: Southeast Collaboratory for Structural Genomics (SECSG) will analyze part of the human genome and the entire genomes of two representative organisms, the euakryotic microorganism, Caenorhabditis elegans and its ancestrally-related and more primitive prokaryotic microbial ancestor, Pyrococcus furiosus. The group emphasizes technology developments, especially for automated steps of X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy techniques.

Supported by: National Institute of General Medical Sciences (NIGMS)/ National Institute of Health (NIH), The Georgia Research Alliance, and The University of Georgia Research Foundation


• Joint Center for Structural Genomics

P.I. : Ian Wilson, Scripps Research Inst.

Description: Joint Center for Structural Genomics (JCSG) is developing high-throughput methods for target selection, protein production, crystallization, and structure determination by X-ray crystallography. JCSG initially focuses on novel structures from C. elegans and on human proteins thought to be involved in cell signaling. It will also cover the structures of similar proteins from other organisms to ensure the inclusion of the greatest number of different protein folds. Five year goal is to generate three-dimensional structures of approximately two thousand proteins.

Supported by: National Institute of General Medical Sciences (NIGMS)/ National Institute of Health (NIH)


• Structural Genomics of Pathogenic Protozoa Consortium

P.I. : Wim Hol, Univ. Washington

Description: The focus of this consortium is development of methods and technologies for determining proteins from pathogenic protozoans, many species of which cause deadly diseases such as Sleeping Sickness (Trypanosoma brucei), Chagas' Disease (Trypanosoma cruzi), Leishmaniasis (Leishmania) and Malaria (Plasmodium falciparum and P. vivax). By using X-ray crystallography, the consortium plans to discover the new folds and design drugs.

Supported by: National Institute of General Medical Sciences (NIGMS)/ National Institute of Health (NIH)


• Center for Eukaryotic Structural Genomics

P.I. : John Markley, Univ. Wisconsin Madison

Description: The center tries to elucidates the three dimensional structures of proteins encoded by Arabidopsis thaliana genome. The initial focus of the center is to develop high-throughput methods for protein production, characterization and structure determination using X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy. This project will facilitate a unique biological research through the study of important model plant.

Supported by: National Institute of GeneralMedical Sciences (NIGMS)/ National Institute of Health (NIH)


• Structure 2 Function Project

P.Is. : John Moult, and Osnat Herzberg, University of Maryland

Description: The project determines structures of hypothetical proteins, i.e., those cannot be related to any previously characterized proteins and, thus, functions of those are unknown. The initial target is selected from Haemophilus influenzae. Structural determination will be done by X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy.

Current Contributors

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