...Miles Graham; Peijun Zhang Developments in cryo-electron microscopy (cryo-EM) have been interwoven with the study of viruses ever since its first applications to biological systems. Following the success of single particle cryo-EM in the last decade, cryo-electron tomography (cryo-ET) is now...

... by the technological advancements in cryo-EM analysis, which has elucidated many new P-type ATPase structures and mechanisms and revealed several new ways of regulation. In this review, we highlight the progress of the field and focus on special features that are present in the five subfamilies. Hence, we outline...

... studies in recent years provide in-depth understanding of how the MLL1 and homologous yeast SET1 complexes interact with the nucleosome core particle (NCP) and how their activities for H3K4 methylation are regulated by the conserved core components. Here, we will discuss the recent single molecule cryo-EM...

... microtubule . Cell 179 , 909 – 22.e12 10.1016/j.cell.2019.09.030 18 Wang , X. , Fu , Y. , Beatty , W.L. , Ma , M. , Brown , A. , Sibley , L.D. et al. ( 2021 ) Cryo-EM structure of cortical microtubules from human parasite Toxoplasma gondii identifies...

... Limited on behalf of the Biochemical Society 2022 cryo-EM membrane proteins palmitoleation WLS Wnt proteins Though sequence similarity between WLS and GPCRs is low (≤ 10%), the Wnt/WLS structures reveal a close resemblance of WLS with the GPCR fold. TM helices 2–8 of WLS align to GPCRs...

... these, the electron cryomicroscopy (cryo-EM) method microcrystal electron diffraction (MicroED) has produced atomic resolution structures of important biological and small molecules. Since its inception in 2013, MicroED established a demonstrated ability for solving structures of difficult samples using vanishingly...

... and distributed under the Creative Commons Attribution License 4.0 (CC BY) . chromatin CMG cryo-EM Ctf18 Pol epsilon replisome In all replicating systems a hexameric, ring-shaped helicase is loaded around DNA and uses the energy derived from nucleotide hydrolysis to unwind the double helix...

...Joshua A. Lees; Joao M. Dias; Seungil Han Electron cryo-microscopy (cryo-EM) is a powerful technique for the structural characterization of biological macromolecules, enabling high-resolution analysis of targets once inaccessible to structural interrogation. In recent years, pharmaceutical...

... structural advances, as well as highlights how the future structural work will further advance our understanding of this enzyme. Figure 2. Structures of human telomerase holoenzyme determined by electron microscopy. ( A ) 30 Å negative stain EM structure. ( B ) 8 Å cryo-EM structure. ( C ) Sub-4 Å cryo...

..., Middle and Tail, was published in 1999. Within the last few years, optimization of Mediator purification combined with technical and methodological advances in cryo-electron microscopy (cryo-EM) have revealed unprecedented details of Mediator subunit organization, interactions with RNA polymerase II...

... adoption of cryo-EM is the expansion of protein target classes for which structural information can drive project decisions, either through an improved mechanistic understanding of disease biology or through high-quality atomistic experimental models of ligand–protein complexes. Perhaps, the best example...

... of the rotor. Figure 2 Subunit interactions about the collar region of the V-ATPase in 3 different conformational states Surface representations of collar subunits based on yeast cryo-EM structures for three rotational states [protein data bank (PDB): 3J9T, 3J9U, 3J9V] showing interactions between...

... implications, with special emphasis on the emerging contributions of cryo-ET. 1 email ruben@biochem.mpg.de 15 1 2016 © 2016 Authors; published by Portland Press Limited 2016 cryo-EM extended-synaptotagmin lipid transfer Orai ryanodine receptor STIM Compartmentalization...