Robert M. Sweet

Robert M. Sweet is the Principal Investigator of the Macromolecular Crystallography Research Resource (PXRR) which provides facilities and support at the National Synchrotron Light Source for the benefit of outside and in-house investigators.   The PXRR is supported by the NIH's National Center for Research Resources and the DOE Office of Biological and Environmental Research in its mission to create optimal facilities and environments for macromolecular structure determination by synchrotron X-ray diffraction.   With a staff of about 24, the PXRR innovates new access modes such as FedEx crystallography, builds new facilities, currently on the X25 undulator, advances automation, develops remote participation software, collaborates with outside groups, teaches novice users, and supports visting investigators with 7day, 20 hours staff coverage.

Research Interests

• Development of techniques and instrumentation for use of synchrotron x-radiation for structural biology.
• Efficient management the Macromolecular Crystallography Research Resource at the NSLS for the benefit of an external users program in macromolecular X-ray crystallography. The BNL News Release of February 12, 2004, describes the extent of this NIH Research Resource grant as well as the parrallel DOE OBER committment.
• Development of fully integrated software for control and monitoring of macromolecular crystallography experiments at synchrotron beam lines.
• Exploring the use of multi-reflection phasing methods in macromolecular crystallography.


        New hybrid in-vacuum undulator for X25

Selected Publications

• Soares A.S., Schneider D.K., Skinner J.M., Cowan M., Buono R., Robinson H.H., Heroux A., Carlucci-Dayton M., Saxena A., and Sweet R.M.
  Remote access to the PXRR macromolecular crystallography facilities at the NSLS.
  Synchrotron Radiation News, 21(5):17-23 (September, 2008).
• Skinner J.M., Cowan M., Buono R., Nolan W., Bosshard H., Robinson H.H., Heroux A., Soares A.S., Schneider D.K. and Sweet R.M.
  Integrated software for macromolecular crystallography synchrotron beamlines II: revision, robots and a database
  Acta Cryst., D62(11):1340-1347 (2006).   PubMed   Full Text
• Robinson H., Soares A.S., Becker M., Sweet R. and Heroux A.
  Mail-in crystallography program at Brookhaven National Laboratory's National Synchrotron Light Source.
  Acta Cryst., D62(11):1336-1339 (2006).   PubMed   Full Text
• Shi W., Robinson H., Sullivan M., Abel D., Toomey J., Berman L.E., Lynch D., Rosenbaum G., Rakowsky G., Rock L., Nolan B., Shea-McCarthy G., Schneider D., Johnson E., Sweet R.M. and Chance M.R.
  Beamline X29: a novel undulator source for X-ray crystallography.
  J Synch Rad., 13:365-372 (2006).   PubMed   Full Text
• Robinson H.H., Shi W., Sullivan M., Nolan W., Schneider D.K., Berman L., Lynch D., Rock L., Rosenbaum G., Johnson E., Chance M.R. and Sweet R.M.
  An undulator beamline for protein crystallography at the NSLS: Commissioning and operation of X29.
  Synch Rad News, 18(5):27-31 (2005).   Full Text
• Jiang J. and Sweet R.M.
  Protein Data Bank depositions from synchrotron sources.
  J Synchrotron Radiat., 11(4):319-327 (2004).   PubMed
• Soares A.S., Caspar D.L., Weckert E., Héroux A., Hölzer K., Schroer K., Zellner J., Schneider D., Nolan W. and Sweet R.M.
  Three beam interference is a sensitive measure of the efficacy of macromolecular refinement techniques.
  Acta Cryst., D59(10):1716-1724 (2003).   PubMed   Full Text
• McGrath W.J., Ding J., Didwania A., Sweet R.M. and Mangel W.F.
  Crystallographic structure at 1.6-A resolution of the human adenovirus proteinase in a covalent complex with its 11-amino-acid peptide cofactor: insights on a new fold.
  Biochim Biophys Acta, 1648(1-2):1-11 (2003).   PubMed
• Retailleau P., Yin Y., Hu M., Roach J., Bricogne G., Vonrhein C., Roversi P., Blanc E., Sweet R.M. and Carter C.W. Jr.
  High-resolution experimental phases for tryptophanyl-tRNA synthetase (TrpRS) complexed with tryptophanyl-5'AMP.
  Acta Cryst., D57(11):1595-1608 (2001).   PubMed
  PDB Files: 1I6K   1I6L   1I6M  
• Chu K., Vojtechovsky J., McMahon B.H., Sweet R.M., Bereendzen J. and Schlichting I.
  Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin.
  Nature, 403:921-923 (2000).   PubMed
  PDB Files: 1DWR   1DWS   1DWT  
• Schlichting I., Berendzen J., Chu K., Stock A.M., Maves S.A., Benson D.E., Sweet R.M., Ringe D., Petsko G.A. and Sligar S.G.
  The catalytic pathway of cytochrome p450cam at atomic resolution.
  Science, 287:1615-1622 (2000).   PubMed
  PDB Files: 1D24   1D26   1D28   1D29  
• Brunori M., Vallone B., Cutruzzola F., Travaglini-Allocatelli C., Berendzen J., Chu K., Sweet R.M. and Schlichting I.
  The role of cavities in protein dynamics: crystal structure of a photolytic intermediate of a mutant myoglobin.
  Proc Natl Acad Sci USA, 97(5):2058-2063 (2000).   PubMed   Full Text
  PDB Files: 1DXC   1DXD  
• Murphy F.V., Sweet R.M., and Churchill M.E.
  The structure of a chromosomal high mobility group protein-DNA complex reveals sequence-neutral mechanisms important for non-sequence-specific DNA recognition.
  EMBO J., 18(23):6610-8 (1999).   PubMed   Full Text
  PDB File: 1QRV  
• Vojtechovsky J., Chu K., Berendzen J., Sweet R.M., Schlichting I.
  Crystal structures of myoglobin-ligand complexes at near-atomic resolution.
  Biophys J., 77(4): 2153-2174 (1999).   PubMed   Full Text
  PDB Files: 1A6G   1A6K   1A6M   1A6N  
• Dautant A., Meyer J.B., Yariv J., Precigoux G., Sweet R.M., Kalb A.F. Frolow F.
  Structure of a monoclinic crystal from of cyctochrome b1 (Bacterioferritin) from E. coli.
  Acta Cryst., D54(1):16-24 (1998).   PubMed
• Skinner J.M. and Sweet R.M.
  Integrated software for a macromolecular crystallography synchrotron beamline.
  Acta Cryst., D54(5):718-725 (1998).   PubMed
• Sweet R.M.
  The technology that enables synchrotron structural biology.
  Nat Struct Biol Suppl., 654-656 (1998).   PubMed
• Wang J., Lim K., Smolyar A., Teng M., Liu J., Tse A.G., Liu J., Hussey R.F., Chishti Y., Thomas C.T., Sweet R.M., Nathenson S.G., Chang H.C., Sacchettini J.C. and Reinherz E.L.
  Atomic structure of an alphabeta T cell receptor (TCR) heterodimer in complex with an anti-TCR fab fragment derived from a mitogenic antibody.
  EMBO J., 17(1):10-26 (1998).   PubMed   Full Text
  PDB File: 1NFD  
• Mangel W.F., Toledo D.L., Ding J., Sweet R.M. and McGrath W.J.
  Temporal and spatial control of the adenovirus proteinase by both a peptide and the viral DNA.
  Trends Biochem Sci., 22(10):393-398 (1997).   PubMed
• Hon W.C., McKay G.A., Thompson P.R., Sweet R.M., Yang D.S., Wright G.D., and Berghuis A.M.
  Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases.
  Cell, 89(6):887-895 (1997).   PubMed
  PDB Files: 1J7U   1J7I   1J7L  
• Hwang K.Y., Song H.K., Chang C., Lee J., Lee S.Y., Kim K.K., Choe S., Sweet R.M., Suh S.W.
  Crystal structure of thermostable alpha-amylase from Bacillus licheniformis refined at 1.7 A resolution.
  Mol Cells, 7(2):251-258 (1997).   PubMed
  PDB Files: 1OB0   1BLI  
• McGrath W.J., Ding J., Sweet R.M. and Mangel W.F.
  Preparation and crystallization of a complex between human adenovirus serotype 2 proteinase and its 11-amino-acid cofactor pVIc.
  J Struct Biol., 117(1):77-79 (1996).   PubMed
• Ding J., McGrath W.J., Sweet R.M. and Mangel W.F.
  Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor.
  EMBO J., 15(8):1778-1783 (1996).   PubMed   Full Text
  PDB File: 1GJL  
• Singer P.T., Smalas A., Carty R.P., Mangel W.F. and Sweet R.M.
  The hydrolytic water molecule in trypsin, revealed by time-resolved Laue crystallography.
  Science, 259:669-673 (1993).   PubMed
  PDB File: 1BTP  
• Sweet R.M., Singer P.T. and Smalas A.
  Considerations in the choice of a wavelength range for white-beam Laue diffraction.
  Acta Cryst., D49:305-307 (1993).   PubMed