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HomeEnvironmentUnlocking the Secrets of Bacterial Resilience: Cryo-EM Mapped Advances

Unlocking the Secrets of Bacterial Resilience: Cryo-EM Mapped Advances

Researchers have discovered the first high-resolution structure of a protein that enables survival in extreme situations, such as exposure to radiation, intense heat, and even the vacuum of space.

A chance meeting at a scientific conference in 2019 led to a significant discovery by researchers at Michigan State University, revealing the first high-resolution structure of proteins that assist in surviving severe conditions, including radiation, heat, and the vacuum of space.

During a 2019 lecture, James K. Billman Endowed Assistant Professor shared research that set the groundwork for this collaborative discovery, which had been developing over many years. In attendance was Professor Emeritus Lee Kroos, who recently concluded his over 30-year career at MSU.

Kroos had been working with colleagues at Spartan to capture the intricate structure of a protein called SpoIVFB (“spo-four-eff-bee”). SpoIVFB is part of a unique group of enzymes that play a vital role in managing essential cellular processes across all forms of life.

This protein is crucial during sporulation, a process that enables bacteria to endure extreme conditions.

Due to the difficulties in capturing SpoIVFB’s structure over the years, Kroos was eager to collaborate with Orlando, who specialists in the innovative technique of cryogenic electron microscopy, or cryo-EM.

“Cryo-EM allows us to observe a level of detail that we cannot achieve with other imaging methods,” Orlando explained.

Now, a study published in Nature Communications by the research teams of Orlando and Kroos presents the first high-resolution experimentally determined structures of SpoIVFB.

The researchers specifically discovered that SpoIVFB attaches to certain molecules, which aids in producing important biochemical substances.

This research sheds light on the mechanisms of cellular regulation that can be found in a wide array of organisms, from bacteria to humans, and has significant implications for fields like microbiology, structural biology, enzymology, and human disease research.

This breakthrough highlights the ongoing $15 million enhancement of advanced cryo-EM facilities at MSU that enables researchers to continually explore new experimental possibilities.

“In recent years, this technology has revolutionized structural biology, particularly in studying membrane proteins,” stated Orlando, who was brought to MSU as part of its Global Impact Initiative — a comprehensive effort aimed at addressing major challenges in energy, health, education, and the environment.

The insights gained from this study will significantly advance structural biology and explore connections to neurodegenerative diseases, various cancers, and metabolic disorders.

Using thousands, or even millions, of images captured from various angles, researchers can develop an extremely detailed three-dimensional representation of the sample being studied.

“This technology has helped us overcome major obstacles, and as it continues to evolve, we will delve deeper into new biological realms,” Orlando remarked, expressing excitement about what the growth of MSU’s cryo-EM facility means for researchers across diverse fields, including materials science, microbiology, and biochemistry.