My lab uses X-ray crystallography to better understand the relationship between proteins and ligands. Tiny differences in the structure of a molecule can radically change the interaction between a protein and ligand and we are only begining to understand how many factors play a role in this interaction. By manipulating the individual components of a compound it is possible to create a chemical that binds to the protein better than the natural substrate, and prevent the natural reaction from occurring. This is the basis for rational drug design. Our efforts have lead us to collaborations with other labs and scientists in many disciplines as our approach to directed compound design has applications not only in basic research but also in pesticide development, health research and clinical research.

selected publications
Academic Articles345
  • Balendiran, G. K., Schnütgen, F., Scapin, G., Börchers, T., Xhong, N., Lim, K., ... Sacchettini, J. C. (2000). Crystal Structure and Thermodynamic Analysis of Human Brain Fatty Acid-binding Protein. JOURNAL OF BIOLOGICAL CHEMISTRY. 275(35), 27045-27054.
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  • McKinney, J. D., zu Bentrup, K. H., Muñoz-Elías, E. J., Miczak, A., Chen, B., Chan, W., ... Russell, D. G. (2000). Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase. NATURE. 406(6797), 735-738.
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  • Sharma, V., Sharma, S., zu Bentrup, K. H., McKinney, J. D., Russell, D. G., Jacobs, W. R., & Sacchettini, J. C. (2000). Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis. Nature Structural and Molecular Biology. 7(8), 663-668.
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  • Lucke, C., Zhang, F., Hamilton, J. A., Sacchettini, J. C., & Ruterjans, H. (2000). Errata. JBIC Journal of Biological Inorganic Chemistry. 267(13), 4312-4312.
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  • Lucke, C., Zhang, F., Hamilton, J. A., Sacchettini, J. C., & Ruterjans, H. (2000). Solution structure of ileal lipid binding protein in complex with glycocholate (vol 267, pg 2929, 2000). European Journal of Biochemistry. 267(13), 4312-4312.
Conference Papers48
chaired theses and dissertations
First Name
Last Name
mailing address
Texas A&M University; Biochemistry & Biophysics; 2128 TAMU
College Station, TX 77843-2128