General Lab Information

Robert Sweet

Scientific Advisor, Structural Biology Program, National Synchrotron Light Source II

Robert Sweet

Brookhaven National Laboratory

National Synchrotron Light Source II
Bldg. 745, Room C08J
P.O. Box 5000
Upton, NY 11973-5000

(631) 344-3401
(631) 338-7302
 rsweet@bnl.gov

Robert Sweet is a Scientific Advisor for NSLS-II's Structural Biology Program. He currently acts as a “Phased Retiree,” editing documents and helping with small research programs. He helped support the case for construction of NSLS-II and then for design and construction of beamlines FMX and AMX. He directed the experimental program there through the start of operations in 2017 to 2019.

Sweet created the first beamline for macromolecular crystallography (MX) at the NSLS in 1984. He led the creation of a consortium of six such beamlines and by 1999 they had won combined support from NIH and DOE to support a staff of about 20 scientists, programmers, and technicians. Together they supported the greatest cohort of users and publications at NSLS. In 1999 he created the popular week-long MX course RapiData, which has continued since 2015 at the SSRL MX facilities.  

Expertise | Research | Education | Publications

Expertise

Crystallography in general.

Many details of macromolecular crystallography 

Experienced in educating young scientists in the physics of x-ray diffraction crystallography.

Research Activities

A range of non-experimental crystallographic subjects.

Education

BS Chemistry Caltech 1965

PhD Physical Chemistry University of Wisconsin, Madison 1970

Selected Publications

  • Schneider DK, Soares AS, Lazo EO, et al (2022) AMX – the highly automated macromolecular crystallography (17-ID-1) beamline at the NSLS-II. Journal of Synchrotron Radiation 29:1480–1494. https://doi.org/10.1107/s1600577522009377
  • Schneider DK, Shi W, Andi B, et al (2021) FMX – the Frontier Microfocusing Macromolecular Crystallography Beamline at the National Synchrotron Light Source II. Journal of Synchrotron Radiation 28:650–665. https://doi.org/10.1107/s1600577520016173
  • Fuchs MR, Sweet RM, Berman LE, et al (2014) NSLS-II Biomedical Beamlines for Macromolecular Crystallography, FMX and AMX, and for X-ray Scattering, LIX: Current Developments. Journal of Physics: Conference Series 493:012021. https://doi.org/10.1088/1742-6596/493/1/012021
  • Héroux A, Allaire M, Buono R, et al (2014) Macromolecular crystallography beamline X25 at the NSLS. Journal of Synchrotron Radiation 21:627–632. https://doi.org/10.1107/s1600577514003415
  • Schneider DK, Berman LE, Chubar O, et al (2013) Three Biomedical Beamlines at NSLS-II for Macromolecular Crystallography and Small-Angle Scattering. Journal of Physics: Conference Series 425:012003. https://doi.org/10.1088/1742-6596/425/1/012003
  • Soares AS, Schneider DK, Skinner JM, et al (2008) Remote Access to the PXRR Macromolecular Crystallography Facilities at the NSLS. Synchrotron Radiation News 21:17–23. https://doi.org/10.1080/08940880802406067
  • Shi W, Robinson H, Sullivan M, et al (2006) Beamline X29: a novel undulator source for X-ray crystallography. Journal of Synchrotron Radiation 13:365–372. https://doi.org/10.1107/s0909049506027853
  • McGrath WJ, Ding J, Didwania A, et al (2003) Crystallographic structure at 1.6-Å resolution of the human adenovirus proteinase in a covalent complex with its 11-amino-acid peptide cofactor: insights on a new fold. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1648:1–11. https://doi.org/10.1016/s1570-9639(03)00024-4
  • Soares AS, Caspar DLD, Weckert E, et al (2003) Three-beam interference is a sensitive measure of the efficacy of macromolecular refinement techniques. Acta Crystallographica Section D Biological Crystallography 59:1716–1724. https://doi.org/10.1107/s0907444903015403
  • Phillips WC, Stanton M, Stewart A, et al (2000) Multiple CCD detector for macromolecular X-ray crystallography. Journal of Applied Crystallography 33:243–251. https://doi.org/10.1107/s0021889899015666
  • Ban N, Freeborn B, Nissen P, et al (1998) A 9 Å Resolution X-Ray Crystallographic Map of the Large Ribosomal Subunit. Cell 93:1105–1115. https://doi.org/10.1016/s0092-8674(00)81455-5
  • Singer PT, Smalås A, Carty RP, et al (1993) The Hydrolytic Water Molecule in Trypsin, Revealed by Time-Resolved Laue Crystallography. Science 259:669–673. https://doi.org/10.1126/science.8430314
  • Ramakrishnan V, Finch JT, Graziano V, et al (1993) Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature 362:219–223. https://doi.org/10.1038/362219a0
  • BLOW DM, JANIN J, SWEET RM (1974) Mode of action of soybean trypsin inhibitor (Kunitz) as a model for specific protein–protein interactions. Nature 249:54–57. https://doi.org/10.1038/249054a0
  • Sweet RM, Wright HT, Janin J, et al (1974) Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6 Å resolution. Biochemistry 13:4212–4228. https://doi.org/10.1021/bi00717a024
  • Sweet RM, Eisenberg D (1983) Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure. Journal of Molecular Biology 171:479–488. https://doi.org/10.1016/0022-2836(83)90041-4
  • Sweet RM, Dahl LF (1970) Molecular architecture of the cephalosporins. Insights into biological activity based on structural investigations. Journal of the American Chemical Society 92:5489–5507. https://doi.org/10.1021/ja00721a032
  • Watson DG, Sweet RM, Marsh RE (1965) The crystal and molecular structure of purine. Acta Crystallographica 19:573–580. https://doi.org/10.1107/s0365110x65003900
Robert Sweet

Brookhaven National Laboratory

National Synchrotron Light Source II
Bldg. 745, Room C08J
P.O. Box 5000
Upton, NY 11973-5000

(631) 344-3401
(631) 338-7302
 rsweet@bnl.gov