Structural Genomics at BNL


      Structural genomics is the systematic determination of 3-dimensional structures of proteins representative of the range of protein structure and function found in nature. The aim, ultimately, is to build a body of structural information that will facilitate prediction of a reasonable structure and potential function for almost any protein from knowledge of its coding sequence. Such information will be essential for understanding the functioning of the human proteome, the ensemble of tens of thousands of proteins specified by the human genome.

      BNL is a member of the New York Structural Genomics Research Consortium (NYSGRC), which is supported by the Protein Structure Initiative of the National Institute of General Medical Sciences (NIGMS) to be a Pilot Structural Genomics Center. Procedures are being developed for high-throughput x-ray crystallography of proteins expressed from cloned genomic or cDNA. Initial targets include a variety of yeast proteins, proteins associated with human disease, and proteins of human pathogens. Protein targets and progress toward structure determination will be posted on the NYSGRC web site.

     BNL is independently taking a structural genomics approach to gain structural information about human proteins that are involved in sensing and repairing DNA damage. This work is supported by the Office of Biological and Environmental Research of the Department of Energy. Protein targets and progress toward structure determination will be posted on this site in the following tables:

Proteins Selected for Expression and Structure Determination

Progress Toward Structure Solution by X-ray Crystallography



Participants in BNL Structural Genomics Efforts

Cloning, Expression and Purification

   F. William Studier
        Helen Kycia
        Nancy Manning
        Eileen Matz

Structure Determination by X-ray Crystallography

   S. Swaminathan
        S. Eswaramoorthy
        D. Kumaran
   Maria Bewley
   John Flanagan
   Jiansheng Jiang

Structures of Membrane Proteins

   Dax Fu
        Brenda V. Daniels

NSLS Crystallography Stations

   Robert Sweet
   Dieter Schneider
   Anand Saxena
   Michael Becker
   Annie Heroux
   Howard Robinson