Education

A.B., Princeton University, 1992
Ph.D., Harvard University, 1999
Lewis Thomas Fellow, Princeton University, 1999-2002
Postdoctoral Fellow, Princeton University, 2002-2004

Courses Taught

• Chemistry 10HS, Honors General Chemistry Seminar
• Chemistry 10H, Honors General Chemistry
• Chemistry 38, Biological Chemistry
• Chemistry 48, Biological Chemistry II
• Chemistry 58, Advanced Experimental Biological Chemistry
• Chemistry 108, Topics in Biochemistry

Publications (Student co-authors underlined)

Torcato, I.M., Kasal, M.R., Brito, P.H., Miller, S.T., Xavier, K.B.  (2019) “Identification of novel AI-2 receptors in Clostridia reveals plasticity in the binding site of the LsrB receptor family.”  J. Biol. Chem.  294 (12), 4450-4463.

Marques, J. C., Oh, I. K., Ly, D. C., Lamosa, P., Ventura, M. R., Miller, S. T., Xavier, K. B.  (2014) “LsrF, a coenzyme A-dependent thiolase, catalyzes the terminal step in processing the quorum sensing signal autoinducer-2.”  Proc. Natl. Acad. Sci. USA 111 (39), 14235–14240.

Rui, F., Marques, J. C., Miller,  S. T., Maycock,  C. D., Xavier,  K. B., & Ventura, M.R. (2012) “Stereochemical diversity of AI-2 analogs modulates quorum sensing in Vibrio harveyi and Escherichia coli.”  Bioorg. Med. Chem. 20 (1), 249-256.

Nicoludis, J. M. Miller, S. T., Jeffrey, P. Barrett, S. P, Rablen, P. R., Lawton, T., Yatsunyk, L. A. (2012) "Optimized end-stacking provides specificity of N-methyl mesoporphyrin IX for human telomeric G-quadruplex DNA" J. Am. Chem. Soc.134 (50), 20446-20456.

Marques, J. C., Lamosa, P., Russell, C., Ventura, R., Maycock C., Semmelhack, M. F., Miller, S. T., and Xavier, K. B.  (2011) "Processing the Interspecies Quorum-sensing Signal Autoinducer-2 (AI-2): Characterization of phospho-(S)-4,5-dihydroxy-2,3-pentanedione isomerization by LsrG protein."  J. Biol. Chem. 287, 18331-18343.

Miller, S. T., Indivero, V. & Burkhard, C. (2009) “Expression and Purification of Sperm Whale Myoglobin.”  J. Chem. Educ.  In Press.

Pereira, C. S., de Regt, A. K., Brito, P. H., Miller, S. T., & Xavier, K. B. (2009) “Identification of Functional LsrB-like Autoinducer-2 Receptors.”  J. Bacteriol.  doi:10.1128/JB.00976-09.

Diaz, Z., Xavier, K. B. & Miller, S. T.  (2009) “The Crystal Structure of the Escherichia coli Autoinducer-2 Processing Protein LsrF.”  PLoS ONE.  4(8), e6820.

Pereira, C., McAuley, J. R., Taga, M. E., Xavier, K. B., & Miller, S. T. (2008) “Sinorhizobium meliloti, a Bacterium Lacking the Autoinducer-2 (AI-2) Synthase, Responds to AI-2 Supplied by Other Bacteria.” Mol. Micro. 70, 1223-1235.

Xavier, K.B., Miller, S.T., Kim, JH, Lu, W., Rabinowitz. J., Pelczer, I., Semmelhack, M.F., Bassler, B. L.  (2007) “Phosphorylation and Processing of the Quorum Sensing Molecule AI-2 in Enteric Bacteria.”  ACS Chemical Biology.  2, 128-136.

Neiditch, M.B., M.J. Federle, S.T. Miller, B.L. Bassler and F.M. Hughson. (2005) “Regulation of LuxPQ Receptor Activity by the Quorum-Sensing Signal Autoinducer-2.” Mol. Cell 18, 507-518.

Miller, S. T., K. Xavier, S. Campagna, M. Taga, M. F. Semmelhack, B. L. Bassler & F. M. Hughson.  (2004) “The Salmonella typhimurium Recognizes a Chemically Distinct Form of the Bacterial Quorum-Sensing Signal AI-2.”  Mol. Cell 15, 677-687.

Das, J., S. T. Miller & D. L. Stern.  (2004) “Comparison of Diverse Protein Sequences of the Nuclear-Encoded Subunits of Cytochrome C Oxidase Suggests Conservation of Structure Underlies Evolving Functional Sites.” Mol. Biol. and Evol. 21, 1572-1582.

Taga, M., S. T. Miller & B. L. Bassler. (2003)  “Lsr-Mediated Transport and Processing of AI-2 in Salmonella typhimurium.”  Mol. Microbiol. 50, 1411-1427.

Miller, S. T., J. M. Hogle & D. J. Filman. (2001)  “Ab initio Phasing of High-Symmetry Macromolecular Complexes: Successful Phasing of Authentic Poliovirus Data to 3.0Å Resolution.”  J. Mol. Biol.  307, 499-512.

Miller, S. T., J. Genova & J. M. Hogle. (1999).  “Collection of Very Low Resolution Protein Data.” J. Appl. Cryst.  32:1183-1185.

Miller, S. T., J. M. Hogle & D. J. Filman. (1996).  “A Genetic Algorithm for the ab initio Phasing of Icosahedral Viruses.”  Acta Crystallographica  D52:235-251.