Directories - Faculty

Department of Biological Science

at Florida State University

Biological Science Faculty Member

Dr. M. Elizabeth Stroupe

  • Office: 202 Kasha Laboratory
  • Office: (850) 644-1751
  • Lab: 218 Kasha Laboratory Building
  • Lab: (850) 645-9317
  • Fax: (850) 644-2259
  • Mail code: 4380
  • E-mail:

Laboratory Home Page

Associate Professor
Ph.D., The Scripps Research Institute, 2002
Graduate Faculty Status

Research and Professional Interests:

What is the relationship between a molecule's structure and its activity in the cell? I am interested in understanding the structure/function relationships driving two pathways: the transformation of a gene into a protein and sulfur metabolism. The two projects in my laboratory are not related topically, but are united in approach. In studying the progression of information from a gene to a protein include, we aim to answer how ribosomes are assembled into functional units. In studying the biochemical basis for sulfur metabolism, we aim to discover how  electrons move from the reductase subunit to the active site of the central sulfur metabolic enzyme sulfite reductase and how sulfite reductase' essential metallic cofactor are synthesized. I use x-ray crystallography and high resoltuion single-particle cryogenic electron microscopy (cryo-EM) to probe across resolutions so I can link atomic resolution details, macromolecular assemblies, and cellular activity.

The lab uses a combination of x-ray crystallography and cryo-EM to determine the structure and function of these important biomolecules.

Selected Publications:

Tavolieri, A. M., Murray, D. T., Askenasy, I., Pennington, J. M., McGarry, L., Stanley, C. B., & Stroupe, M. E. (2019). NADPH-Dependent  Sulfite Reductase Flavorprotein Adopts an Extended Conformation Unique to this Diflavin Reductase. J. Struct. Biol., 205, 170-179. Retrieved from

Askenasy, I., Murray, D. T., Andrews, R. M., Uversky, V. N., He, H. & Stroupe, M. E. (2018). Structure-Function Relationships in the Oligomeric NADPH-Dependent Assimilatory Sulfite Reductase. Biochemistry, 57, 3764-3772. Retrieved from

Cepeda, M. R., McGarry, L., Pennington, J. M., Krystek, J., & Stroupe, M. E. (2018). The role of extended Fe4S4 cluster ligands in mediating sulfite reductase hemoprotein activity. Biochimi Biophys Acta Proteins Proteom., 1866, 933-940. Retrieved from

Stroupe, M. E., & Warren, M. J. (2017). Siroheme assembly and insertion to Nitrite and Sulfite Reductase. In
Johnson, M. K, & Scott, RA. . (Eds.), Encyclopedia of Inorganic and Bioinorganic Chemistry: Metalloprotein Site Assembly. Chichester. Retrieved from

Johnson, M. C., Sena-Velez, M., Washburn, B. K., Platt, G. N., Lu, S., Brewer, T. E., Lynn, J. S., Stroupe, M. E., & Jones, K. M. (2017). Structure, proteome and genome of Sinorhizobium meliloti phage ΦM5: A virus with LUZ24-like morphology and a highly mosaic genome. J. Struct. Biol, 200, 343-359. Retrieved from

Johnson, M. C., Ghalei, H., Doxtader, K. A., Karbstein, K., & Stroupe, M. E. (2017). Structural Heterogeneity in Pre-40S Ribosomes. Structure, 25, 329-340. Retrieved from

Khoshnevis, S., Askenasy, I., Johnson, M. C., Dattolo, M. D., Young-Erdos, C. L., Stroupe, M. E., & Karbstein, K. (2016.) The DEAD-box Protein Rok1 Orchestrates 40S and 60S Ribosome Assembly by Promoting the Release of Rrp5 from Pre-40S Ribosomes to Allow for 60S Maturation. PLoS Biology. Retrieved from:


Johnson, M. C., Tatum, K. B., Lynn, J. S., Brewer, T. E., Washburn, B. K., Stroupe, M. E., & Jones, K. M. (2015). Sinorhizobium meliloti phage ΦM9 defines a new group of T4-superfamily phages with unusual genomic features, but a common T=16 capsid. Journal of Virology, 10945-10958. Retrieved from

Askenasy, I., Pennington, J. M., Tao, Y., Marshall, A. G., Young, N. L., Sheng, W., & Stroupe, M. E. (2015). The N-terminal Domain of Escherichia coli Assimilatory NADPH-Sulfite Reductase Hemoprotein Is an Oligomerization Domain that Mediates Holoenzyme Assembly. Journal of Biological Chemistry, 290, 15. Retrieved from

Ghalei, H., Schaub, F., Doherty, J., Roush, W. R., Cleveland, J. J., Stroupe, M. E., & Karbstein, K. (2015). Hrr25/CK1δ-directed release of Ltv1 from pre-40S ribosomes is necessary for ribosome assembly and cell growth. The Journal of Cell Biology, 208, 745-759. Retrieved from

Kopylov, M., Bass, H. W., & Stroupe, M. E. (2015). Identification and characterization of a plant G-quadruplex-binding protein encoded by the maize (Zea mays L.) nucleoside diphosphate kinase1 gene, ZmNDPK1. Biochemistry, 54, 1743-1757. Retrieved from

Andorf, C. M., Kopylov, M., Dobbs, D., Koch, K. E., Stroupe, M. E., Lawrence, C. J., & Bass, H. W. (2014). G-Quadruplex (G4) Motifs in the Maize (Zea mays L.) Genome Are Enriched at Specific Locations in Thousands of Genes Coupled to Energy Status, Hypoxia, Low Sugar, and Nutrient Deprivation. J Genet Genomics, 12, 627-647. Retrieved from 

Brewer, T., Stroupe, M. E., & Jones, K. M. (2014). The genome, proteome and phylogenetic analysis of Sinorhizobium meliloti phage ΦM12, the founder of a new group of T4-superfamily phages. Virology, 450-451, 84-97. Retrieved from

Stroupe, M. E., Brewer, T., Sousa, D. R., & Jones, K. M. (2014). The structure of Sinorhizobium meliloti phage ΦM12, which has a novel T=19l triangulation number and is the founder of a new group of T4-superfamily phages. Virology, 450-451, 205-212. Retrieved from

Sousa, D. R., Stagg, S. M., & Stroupe, M. E. (2013). Cryo-EM structures of the actin:tropomyosin filament reveal the mechanism for the transition from C- to M-state. J Mol Biol, 425(22), 4544-55. Retrieved from

Smith, K. W., & Stroupe, M. E. (2012). Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer. Biochemistry, 51(49), 9857-68. Retrieved from

Postdoctoral Associates:

Rai, Jay

Graduate Students:

Murray, Daniel

: External sites will open in a new browser window.