News

2 Jun 2020

Emerging Topics in Biomolecular Magnetic Resonance – A new on-line lecture series

A new on-line lecture series on Emerging Topics in Biomolecular Magnetic Resonance, organized by Loren Andreas, Stefan Glöggler, Christian Griesinger, Mei Hong, Oscar Millet, Art Palmer, and Markus Zweckstetter, starts on Thursday, June 4, 2020.

1 Jun 2020

Cryo-EM reaches yet another milestone – Comments on two recent cryo-EM atomic resolution studies

Two studies published during last two weeks have reported that single particle cryo-EM data can be now resolved to 1.20Å or 1.25Å, respectively. The groups of Sjors H.W. Scheres (LMB-MRC, Cambridge) and Holger Stark (MPI Göttingen) have for the first time shown that atomic resolution is attainable by single particle cryo-EM.

27 May 2020

EOSC-Life Training Call Opportunity

The EOSC-Life Training team offers funding to support training activities and provides expertise and guidance to help you organise successful and impactful training through our Training Open Call.

27 May 2020

Single-particle cryo-EM at atomic resolution

A. Radu Aricescu & Sjors H.W. Scheres et al. show in the bioRxiv paper that using a new electron source, energy filter and camera, a 1.7 Å resolution cryo-EM reconstruction for a prototypical human membrane protein, the β3 GABAA receptor homo-pentamer, can be obtained.

25 May 2020

Breaking the next Cryo-EM resolution barrier – Atomic resolution determination of proteins!

In a new bioRxiv paper, Holger Stark et a. report a 1.25 Å resolution structure of apoferritin obtained by cryo-EM with a newly developed electron microscope providing unprecedented structural details. Their apoferritin structure has almost twice the 3D information content of the current world record reconstruction (at 1.54 Å resolution). For the first time in cryo-EM they can visualize individual atoms in a protein, see density for hydrogen atoms and single atom chemical modifications.

18 May 2020

PostEra Call: Help us Fight Coronavirus - Contribute your expertise to design inhibitors of the SARS-CoV-2 main protease

An international group of scientists from academia and industry is seeking opportunities to contribute to combatting COVID-19. They welcome contributions of many forms including scientific expertise, experimental capabilities, and indeed donations to make this possible.

Highlights of Coronavirus Structural Studies

5 May 2020

Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein

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.

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1 Jan 2017

Newsletter 1/2017

Reader's Corner Archive

TIP

30 Jul 2019

Principles for Integrative Structural Biology Studies

Guru of integrative structural biology computation Andrej Sali and Michale P. Rout summarize in the recent Cell Primer Principles for Integrative Structural Biology Studies.

Visualization of biological macromolecules at near-atomic resolution: cryo-electron microscopy comes of age

The topical review by Alok K. Mitra recapitulates developments and transformational advances of cryo-EM technology.

16 Jul 2019

The expanding toolkit for structural biology: synchrotrons, X-ray lasers and cryo-EM

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.