The new cryoPRISM method allows researchers to observe biomolecular complexes in a quick, accurate, and budget-friendly way, providing new insights into bacterial protein synthesis.

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MIT News

Researchers at MIT have developed cryoPRISM (purification-free ribosome imaging from subcellular mixtures), a new structural biology technique that allows visualization of biomolecular complexes in near-native cellular conditions. The method works by imaging molecules from freshly lysed cells rather than fully purified samples, preserving natural molecular interactions while still achieving sufficient resolution. Discovered serendipitously from an unexpected negative control result, cryoPRISM validated known ribosomal states and uncovered novel ones — including an interaction between hibernating ribosomes and elongation factor EF-G in bacteria, previously only observed in more complex organisms. The technique is faster and more cost-effective than traditional in-cell imaging and is already being applied to difficult-to-culture organisms like pathogens and patient-derived red blood cells.

CryoPRISM: A new tool for observing cellular machinery in a more natural environment