An optimized 3D fluorescence co-localization method is a useful toolkit to obtain cellular 3D separations between green and red labeled protein domains with nanometer-scale accuracy using light microscopy.
Structural and biochemical analysis of an abundant and conserved protein complex called EMC shows how it is likely to insert nascent membrane proteins into the endoplasmic reticulum membrane.
High-resolution optical microscopy is used to reveal the organization of extracellular matrix proteins within the basement membrane of the blood filtration barrier in the kidney at the nanometer scale.
The first structures of Kaposi’s sarcoma-associated herpesvirus ORF68 and Epstein–Barr virus BFLF1, conserved and essential proteins required in herpesviruses, reveal new insights into viral genome packaging.
The structural architecture of the 4-subunit, RNA-binding human negative elongation factor NELF is derived by a combination of X-ray crystallography and protein crosslinking.
The cryo-EM structures of XKR9 define the architecture and caspase-mediated activation of a protein family that is involved in the exposure of phosphatidylserine during apoptosis leading to the engulfment of apoptotic cells by macrophages.
In Thermoplasma acidophilum, an archaeon without histones, a DNA-binding protein acquired from bacteria via horizontal gene transfer mediates histone-like chromatin architecture.
