CryoPRISM imaging launched
MIT unveiled cryoPRISM, a lower‑cost platform for observing biomolecular complexes in near‑native states—promising sharper cellular machinery imaging for molecular research. While early work targets bacterial protein synthesis, the platform could accelerate molecular cytology research by improving visualization of protein complexes in pathological specimens. (news.mit.edu)
CryoPRISM’s lead authors are Mira B. May and Gabriella S. Lopez‑Perez from Joey H. Davis’s lab at MIT, and the work is listed with DOI 10.1073/pnas.2521210123 in the Proceedings of the National Academy of Sciences. The name cryoPRISM expands to “purification‑free ribosome imaging from subcellular mixtures,” and the published workflow explicitly combines cell lysis, rapid vitrification of lysates, and single‑particle image‑analysis pipelines. Authors deposited the raw cryo‑EM data set as EMPIAR‑13232 consisting of 9,748 multi‑frame micrographs (45 frames each) with an imageset size of 2.38 TB, released to public repositories on Feb 13, 2026. Application of the method to Escherichia coli lysates produced over 20 distinct ribosomal structural states and a 2.9‑Å reconstruction for a complex showing elongation factor G (EF‑G) and ribosome‑associated inhibitor A (RaiA) bound simultaneously (PDB entry 9PYC). The cryoPRISM protocol first appeared as a bioRxiv preprint on Aug 21, 2025 and was later peer‑reviewed and published in PNAS in early March 2026, documenting the transition from preprint to archived peer‑reviewed record. The authors report that by avoiding biochemical purification steps, cryoPRISM preserves native protein–protein contacts while still yielding high‑resolution classes, and they provide downloadable micrograph sets and coordinates to enable independent reanalysis by laboratories with cryo‑EM access.
