Thus, bioconjugation chemistry is no longer the limiting factor for multiplex cell surface protein imaging.

In conclusion, we have unveiled a previously unrecognized domainization principle of the chromatin, encoded by nucleosome wrapping states.

Our findings not only provide valuable insights into the structural roles of glycans in bio-assemblies but also demonstrate the potential of our recently formulated research strategy of CryoSeek to find bioentities and establish prototypes for structural studies of carbohydrates.

In conclusion, NanaPPI provides a robust, easy, and economical method for rapid in situ measurement of PPIs in cells and tissues, which has great potential for new PPI identification, PPI inhibitor screening, and PPI biomarker-based diagnosis in clinics.

Here, we report a cryo-EM structure of the heavily glycosylated Chlamydomonas mastigoneme at 2.3-2.5 angstrom resolutions. In addition to enabling analysis of accurate interactions for glycosyl packing, the high resolution map reveals an unprecedented 5',5'-phosphodiester bond that links adjacent glycan chains attached to hydroxyproline (Hyp) residues n and n+3. Structural analysis reveals a secondary structural element for glycoconjugates, which we name the poly-Hyp (pHP) glycohelix. Our work represents an important advancement in deciphering glycan folding.

The proposed hybrid detector concept was verified, and a prototype detector showed high performance for 3D positioning and timing resolution. The novel detector concept shows promise for preclinical and clinical PET scanners with DOI capability.