The ability of single particle cryo-electron microscopy to capture structural information on samples that could not be crystallized for use with crystallographic methods or were too delicate for ...
Cryo-electron microscopy (cryo-EM) reached single-atom resolution for 3D structure determination of biological macromolecules. Cryo-EM has been determining the structures of protein structures for ...
SPOP is the most mutated protein in prostate cancer and plays a role in endometrial, uterine and other cancers. Despite this importance, how SPOP mutations drive cancer has been incompletely ...
The first molecular-level structural analysis of the Omicron variant spike protein in complex with human ACE2 is now available. The near-atomic resolution analysis—using cryo-electron ...
Our bodies comprise different tissues and organs, which are composed of many cells that must adhere to form functional higher order structures. This adherence is facilitated by specialized proteins ...
Electron microscopy allows researchers to visualize the morphological effects of biological, genetic, and physical perturbations by diving into tissues and cells. Images collected on our microscopes ...
Temporary protein-protein bonds are essential for processes including enzymatic reactions, antibody binding, and response to medication. Being able to accurately characterize these bonds is important ...
Cryo-EM is referred to as a form of EM where a transmission electron microscope (TEM) is used to obtain the image of radiation-sensitive specimens under cryogenic conditions. The phrase cryo-EM is ...
Healthy cells are constantly breaking down proteins and building up new ones with the help of enzymes aptly named unfoldases, because they unravel proteins tagged for destruction or recycling. Now, a ...
Images created with the new FLASH-PAINT microscopy technique, developed at Yale by the laboratory of Joerg Bewersdorf, PhD. Credit: Bewersdorf Laboratory, Yale University Images created with the new ...
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