Title (All Applicants)
Project Advisor(s) (Students Only)
Dr. Andrzej Joachimiak, Argonne National Laboratory, Cathy Hatzos-Skintges, Argonne National Laboratory
Presentation Type (All Applicants)
Oral Presentation
Disciplines (All Applicants)
Biochemistry | Biology | Molecular Biology | Structural Biology
Description, Abstract, or Artist's Statement
New Delhi metallo-β-lactamase-1 is a problematic gene found in certain strains of bacteria that cause them to become antibiotic resistant to nearly all known antibiotics. While some antibiotics are available to treat patients with a bacterial infection, most are toxic or do not have 100% success rates. With that being said, it is imperative that we search for a molecule that is successfully able to inhibit the effects of this gene every time. Such a discovery would help tremendously with new antibiotic drug development and also prevent further damage by these dangerous bacteria. In this presentation, I will describe the purification process for proteins expressed by the NDM-1 gene that we crystallized by dissolving them in our desired inhibitor, NZ218. Once the crystals were sizable enough for analysis, we cryo-protected the crystals and observed their protein structures using X-ray crystallography. In particular, we examined the structures closely for the presence of the NZ218 inhibitor in the active site.
Augustana Digital Commons Citation
Wills, Brandon M.. "Purification, Optimization, and Growth of New Delhi metallo-β-lactamase-1 protein crystals mixed with NZ218 inhibitor" (2016). Celebration of Learning.
https://digitalcommons.augustana.edu/celebrationoflearning/2016/presentations/3
Included in
Biochemistry Commons, Biology Commons, Molecular Biology Commons, Structural Biology Commons
Purification, Optimization, and Growth of New Delhi metallo-β-lactamase-1 protein crystals mixed with NZ218 inhibitor
New Delhi metallo-β-lactamase-1 is a problematic gene found in certain strains of bacteria that cause them to become antibiotic resistant to nearly all known antibiotics. While some antibiotics are available to treat patients with a bacterial infection, most are toxic or do not have 100% success rates. With that being said, it is imperative that we search for a molecule that is successfully able to inhibit the effects of this gene every time. Such a discovery would help tremendously with new antibiotic drug development and also prevent further damage by these dangerous bacteria. In this presentation, I will describe the purification process for proteins expressed by the NDM-1 gene that we crystallized by dissolving them in our desired inhibitor, NZ218. Once the crystals were sizable enough for analysis, we cryo-protected the crystals and observed their protein structures using X-ray crystallography. In particular, we examined the structures closely for the presence of the NZ218 inhibitor in the active site.