Robert M. Sweet

Biology Department, 463
Brookhaven National Laboratory
Upton, NY 11973-5000

tel: (631) 344-3401
fax: (631) 344-2741
sweet@bnl.gov

The Group in 2004:
Robert Sweet (631) 344-3401
Rick Buono (631) 344-3005
Matt Cowan (631) 344-4210
Sal Sclafani (631) 344-5055
John Skinner (631) 344-3222
Grace Shea-McCarthy (631) 344-7411


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


Publications:
Skinner JM, Cowan M, Buono R, Nolan W, Bosshard H, Robinson HH, Heroux A, Soares AS, Schneider DK, and Sweet RM.
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 AS, 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 LE, Lynch D, Rosenbaum G, Rakowsky G, Rock L, Nolan B, Shea-McCarthy G, Schneider D, Johnson E, Sweet RM, and Chance MR.
Beamline X29: a novel undulator source for X-ray crystallography.
J Synch Rad 13, 365-372 (2006).   PubMed   Full Text
Robinson HH, Shi W, Sullivan M, Nolan W, Schneider DK, Berman L, Lynch D, Rock L, Rosenbaum G, Johnson E, Chance MR, and Sweet RM.
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 RM.
Protein Data Bank depositions from synchrotron sources.
J Synchrotron Radiat. 11(4), 319-327 (2004).   PubMed
Soares AS, Caspar DL, Weckert E, Héroux A, Hölzer K, Schroer K, Zellner J, Schneider D, Nolan W, and Sweet RM.
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 WJ, Ding J, Didwania A, Sweet RM, and Mangel WF.
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 RM, and Carter CW 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 BH, Sweet RM, 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 AM, Maves SA, Benson DE, Sweet RM, Ringe D, Petsko GA, and Sligar SG.
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 RM, 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 FV, Sweet RM, and Churchill ME.
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 RM, 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 JB, Yariv J, Precigoux G, Sweet RM, Kalb AF, Frolow F.
Structure of a monoclinic crystal from of cyctochrome b1 (Bacterioferritin) from E. coli.
Acta Cryst. D54(1), 16-24 (1998).   PubMed
Skinner JM and Sweet RM.
Integrated software for a macromolecular crystallography synchrotron beamline.
Acta Cryst. D54(5), 718-725 (1998).   PubMed
Sweet RM.
The technology that enables synchrotron structural biology.
Nat Struct Biol Suppl. 654-6 (1998).   PubMed
Wang J, Lim K, Smolyar A, Teng M, Liu J, Tse AG, Liu J, Hussey RF, Chishti Y, Thomas CT, Sweet RM, Nathenson SG, Chang HC, Sacchettini JC, and Reinherz EL.
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 WF, Toledo DL, Ding J, Sweet RM, and McGrath WJ.
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 WC, McKay GA, Thompson PR, Sweet RM, Yang DS, Wright GD, and Berghuis AM.
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 KY, Song HK, Chang C, Lee J, Lee SY, Kim KK, Choe S, Sweet RM, Suh SW.
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 WJ, Ding J, Sweet RM, and Mangel WF.
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 WJ, Sweet RM, and Mangel WF.
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 PT, Smalas A, Carty RP, Mangel WF, and Sweet RM.
The hydrolytic water molecule in trypsin, revealed by time-resolved Laue crystallography.
Science 259, 669-673 (1993).   PubMed
PDB File: 1BTP  
Sweet RM, Singer PT, and Smalas A.
Considerations in the choice of a wavelength range for white-beam Laue diffraction.
Acta Cryst. D49, 305-307 (1993).   PubMed
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