Instruct-ERIC Training call now open
Call for proposals for Instruct Centre Training Courses to be held in 2020 is now open.
CIISB 2020 - A Short Outlook into the Foreseeable Future in 6654 Characters
On January 31, 2020 CIISB has submitted the final report of the MEYS large infrastructure support project LM 2015043, which financed its operation during the years 2016-2019. The final report contains also a short description and outlook of the CIISB activities in the upcoming period.
Pilot Version of On-line Submission System for Open Access requests to CIISB Core Facilities
So far, all requests for Open Access to CIISB Core facilities required submission of filled paper forms via email. Since January 2020, new on-line submission system offers simplified protocol for submission of requests for open access to all ten CIISB Core Facilities.
6th European Crystallography School in Budapest
Registration to the 6th European Crystallography School to be held in Budapest, Hungary, between 5 and 11 July 2020 is now open.
The Instruct-ERIC Training Programme for 2020 is now online
Every year, Instruct-ERIC organises a programme of training events. These hands-on workshops cover a range of cutting-edge methods in structural biology to enable scientists to expand their expertise and implement new techniques in their research. Instruct training courses are delivered by world-renowned experts.
EU invests 10 million euro in unlocking technologies for key research in structural biology
To enable researchers from European institutes to extend innovative structural biology research, the EU has invested 10 million euro to iNEXT-Discovery, through its Horizon 2020 program.
Highlights of Coronavirus Structural Studies
Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by Remdesivir
The pandemic of Corona Virus Disease 2019 (COVID-19) caused by SARS-CoV-2 has become a global crisis. The replication of SARS-CoV-2 requires the viral RNA-dependent RNA polymerase (RdRp), a target of the antiviral drug, Remdesivir. In the Science paper (published May 1, 2020) Yechun Xu, Shuyang Zhang, Yan Zhang, and H. Eric Xu report the cryo-EM structure of the SARS-CoV-2 RdRp either in the apo form at 2.8 Å resolution or in complex with a 50-base template-primer RNA and Remdesivir at 2.5 Å resolution. The complex structure reveals that the partial double-stranded RNA template is inserted into the central channel of the RdRp where Remdesivir is covalently incorporated into the primer strand at the first replicated base pair and terminates chain elongation. The obtained structures provide critical insights into the mechanism of viral RNA replication and a rational template for drug design to combat the viral infection.
Crystal structure of Nsp15 endoribonuclease NendoU from SARS-CoV-2
Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) is rapidly spreading around the world. There is no existing vaccine or proven drug to pre- vent infections and stop virus proliferation. Although this virus is similar to human and animal SARS-CoVs and Middle East Respiratory Syndrome coronavirus (MERS-CoVs), the detailed information about SARS-CoV-2 proteins structures and functions is urgently needed to rapidly develop effective vaccines, antibodies, and antivirals. Andrzej Joachimiak et. al applied high-throughput protein production and structure determination pipeline at the Center for Structural Genomics of Infectious Diseases, Argonne National Laboratory, to produce SARS-CoV-2 proteins and structures. In the Protein Science paper they report two high-resolution crystal structures of endoribonuclease Nsp15/NendoU and compare these structures with previously reported homologs from SARS and MERS coronaviruses.
Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for severe acute respiratory syndrome– coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious coronavirus disease 2019 (COVID-19) epidemic. The Science article by Qiang Zhou et. al. presents cryo–electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B0AT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface. The ACE2-B0AT1 complex is assembled as a dimer of heterodimers, with the collectrin-like domain of ACE2 mediating homodimerization. The RBD is recognized by the extracellular peptidase domain
of ACE2 mainly through polar residues. These findings provide important insights into the molecular basis for coronavirus recognition and infection.
Reader's Corner Archive
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.
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.