6th Open Call for Instruct-ERIC Internships
Annually presented price for outstanding work published in the area of nuclear magnetic resonance in memory of Petr Sedmera, a renowned scientist who greatly contributed to the development of the field.
The new instrument equipped at the Proteomics Core Facility, CEITEC MU.
We build branched DNA species that can be joined using Watson-Crick base pairing to produce N-connected objects and lattices. We have used ligation to construct DNA topological targets, such as knots, polyhedral catenanes, Borromean rings and a Solomon's knot.
This course/workshop allowed participants, with some prior knowledge and experience in macromolecular crystallography, to access the biophysical measurements section and the crystal handling/X-ray diffraction section of the Instruct CZ / CIISB CMS core facility for three practical work sessions.
The emergence of SARS-CoV-2 has resulted in >90,000 infections and >3,000 deaths. Coronavirus spike (S) glycoproteins promote entry into cells and are the main target of antibodies. We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, correlating with the efficient spread of SARS-CoV-2 among humans. We found that the SARS-CoV-2 S glycoprotein harbors a furin cleavage site at the boundary between the S1/S2 subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and SARS-related CoVs. In the study published in Cell, David Veesler with coworkers determined cryo-EM structures of the SARS-CoV-2 S ectodomain trimer, providing a blueprint for the design of vaccines and inhibitors of viral entry. Finally, they demonstrate that SARS-CoV S murine polyclonal antibodies potently inhibited SARS-CoV-2 S mediated entry into cells, indicating that cross-neutralizing antibodies targeting conserved S epitopes can be elicited upon vaccination.
The topical review by Alok K. Mitra recapitulates developments and transformational advances of cryo-EM technology.
Samar Hasnain et. al. describe the steadily-expanding methodologies for atomic resolution studies in The expanding toolkit for structural biology: synchrotrons, X-ray lasers and cryo-EM. Of note is the following statistics: Despite the wealth of structures in the Protein Data Bank, a closer examination reveals that 89% of the structures, i.e. 126 994, are of proteins or complexes with a molecular weight of less than 160 kDa. Furthermore, only 4% of the deposited structures have a molecular weight in excess of 300 kDa.