Project Advisor(s)

Dr. Andrzej Joachimiak, Argonne National Laboratory, Cathy Hatzos-Skintges, Argonne National Laboratory

Presentation Type

Oral Presentation

Disciplines

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.

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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.