Looking at the precise 3D arrangement of atoms within a protein helps us to understand how it can perform its functions. Radu Aricescu’s and Sjors Scheres’ groups have now been able to resolve individual atoms for the first time in a three-dimensional cryo-EM image.
Specimen movement reduces the quality of structural data produced by cryo-EM. Chris Russo’s group presents a physical theory for the causes of this movement, and creates a new specimen support that eliminates it.
Venki Ramakrishnan’s group has solved the structure of the protein complex formed when mRNA is being scanned to find the start codon, providing new understanding of the molecular mechanisms underpinning initiation of translation.
John Briggs’ group has led two new studies of the spike (S) protein that mediates binding to the receptor ACE2 and is the dominant target of the immune system, with applications for development of vaccines and diagnostic tests.
Abnormal filaments of α-synuclein define several neurodegenerative diseases, including multiple system atrophy (MSA) and Parkinson’s disease. Michel Goedert’s and Sjors Scheres’ groups have now determined the first structures of α-synuclein filaments from human brain.
Every time a cell divides, all of its genetic material must be accurately duplicated. This process is controlled by a molecular machine known as the replisome. Joseph Yeeles’ group has now produced the highest resolution, and most complete, structure of a replisome to date.