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2019 Workshop on Advances and Challenges of Biological CryoEM


(High resolution video can be accessed here: https://cryoem101.org/chapter-1/)

The recent integration of new developments in electron microscopes, direct electron detection cameras, and advances in image analysis methods are allowing the expansion of high resolution structural molecular biology in new and exciting directions by direct visualization of macromolecules and their complexes. The next decades will be dominated by the study of protein-protein, protein-nucleic acid complexes, molecular machines, and their conformational changes in ways that were impossible before due to their size and/or the need to study them in crystalline form. In addition, developments in many aspects of electron microscopy are providing new tools for the study of biological molecules from the single molecule to the cellular level. The inaugural workshop on Advancement and Challenges of Biological CryoEM will address key developments in this fast advancing field, provide an opportunity to discuss the state of the field and exchange views on advancement and challenges of biological cryo-electron microscopy, and foster the research collaboration of biological and biomedical sciences, particularly in Hong Kong, China, and Asia. The workshop will be hold the day after the GRC Conference on three-dimension electron microscopy in Hong Kong, which is the premier cryoEM meeting, to encourage the participation of GRC attendees.

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Third Coast Workshop on Biological Cryo-EM announced for May 19, 2018

March 19, 2018 • 9:00am – 6:00pm
Gordon Center for Integrative Science, University of Chicago

 

Friends,

As announced a few months ago, a new version of our very successful Third Coast cryo-EM Workshop is being programmed for May 19th at the Gordon Center for Integrative Sciences at the University of Chicago.

Following last year format, we will have a full day of talks and discussions led by key luminaries in the application of cryo electron microscopy and associated computational approaches to the structure of macromolecules, macromolecular complexes and subcellular structures. In this version of the program (included below) we are privileged to have Prof. Michael Rossmann (Purdue University) as this year’s keynote lecturer.

The website is now live at http://memprotein.org/cryoem-workshop and includes a registration link. There is no cost to attend the Workshop. However, this year, we will close the registration process as soon as the capacity of the auditorium is reached. For that reason, we strongly encourage you to register early, given the unexpected (overwhelming!) response last year. Furthermore, we strongly encourage all attendants to submit posters for discussion during the Workshop. This is a fantastic opportunity to show your work to a receptive community, whether it is ready for prime time, or not.

Given the stellar roster of speakers, we expect to have an exciting workshop where the key cryo-EM topics of the moment will be presented and debated. Personally, we are very much looking forward to seeing you and interacting with you later in May.

All the best,

The Organizing Committee

Eduardo Perozo
Alfonso Mondragon
Valerie Tokars
Bobby Kasthuri

Program, registration, and poster at the website: http://memprotein.org/cryoem-workshop/

Emad Tajkhorshid and co-PIs at UIUC recipients of NIH High-Risk, High-Reward Research

University of Illinois professor and MPSDC team member Emad Tajkhorshid, along with co-PIs Chad Rienstra (Chemistry) and James Morrissey (Biochemistry) have been awarded a Director’s Transformative Research Award from the National Institutes of Health for their highly creative approach to the study of cell membrane lipids.

Membrane proteins are abundant in eukaryotic cells and play important roles in a great many biological processes ranging from cell adhesion and recognition to energy production to signaling cascades. 

Membrane proteins make up more than half of the targets for currently approved drugs, which underscores their relevance to human disease but less is known about the membrane lipids that interact with proteins and ligands.

It is becoming increasingly clear that lipids are effector molecules that modulate and/or directly carry out essential biological functions at very different rates depending on what types of lipids are present. Some examples include blood clotting, cell recognition (in immunological response especially), ion conduction (important for neuronal function and viral infection), transport of drugs across the membrane, and pain response.

A potential long-term application is the development of more effective drugs that target biological membranes. Since about 60% of the drugs on the market target membrane-bound proteins, a better understanding of lipid structure and dynamics could greatly improve the efficacy of drug design efforts by modeling the interactions that take place. This would have broader impacts on understanding all the biological functions above and potentially to address the resulting pathologies or diseases. Better blood thinners would help to ameliorate deep vein thrombosis, heart attacks and strokes. Improved modeling of immunological cell recognition and viral life cycles would help to address infectious diseases ranging from influenza to HIV/AIDS. Understanding how drugs are transported would aid in the development of better antibiotics. The project aims to develop a toolkit of methods that would be available to researchers addressing this range of problems and many others.

The High-Risk, High-Reward Research (HRHR) program, supported by the National Institutes of Health (NIH’s Common Fund) awarded twelve transformative research awards funded by the Director’s office. The awards span the broad mission of the NIH and include groundbreaking research.

Read more about the project here: link

In memory: Klaus Schulten

Klaus Schulten, professor of physics and Beckman Institute faculty member for nearly 25 years, has died after an illness. Schulten, who led the Theoretical and Computational Biophysics Group, was a leader in the field of biophysics, conducting seminal work in the area of molecular dynamics simulations, illuminating biological processes and structures in ways that weren’t possible before. His research focused on the structure and function of supramolecular systems in the living cell, and on the development of non-equilibrium statistical mechanical descriptions and efficient computing tools for structural biology. Schulten received his Ph.D. from Harvard University in 1974. At Illinois, he was Swanlund Professor of Physics and was affiliated with the Department of Chemistry as well as with the Center for Biophysics and Computational Biology; he was Director of the Biomedical Technology Research Center for Macromolecular Modeling and Bioinformatics as well as Co-Director of the Center for the Physics of Living Cells.

A memorial service and reception was held November 7. The Beckman Institute will host an honorary symposium in 2017.

Benoît Roux, PI of the MPSDC Computational Modeling Core of which Schulten was an active contributor, shares the following words:

Understanding how biological macromolecular systems (proteins, nucleic acids, membranes) function in terms of their atomic structure represents an outstanding challenge for computational chemists and biophysicists. In this regards, the groundbreaking achievements of Klaus Schulten in Biophysics have opened the door to an unprecedented understanding of biological macromolecular machines. Thanks to the pioneering work of Klaus Schulten, models rigorously anchored in physical laws are now an intrinsic part of life sciences. Because of his intellectual leadership, the complexity of biological systems that can be simulated goes well beyond anything one would have dreamed just a few years ago. By his outstanding contributions, Klaus Schulten has changed the paradigm of computational science and molecular dynamics simulations of complex molecular systems. His tragic loss will long resonate throughout our community.

But Klaus was more than a great scientist, for many of us he was also a close friend. He was great company, and a very collegial and generous member of our community. We will cherish all these memories with him forever.

Solving a Major Piece of a Cellular Mystery about Nuclear Pore Complexes

Drs. Shohei Koide and Anthony Kossiakoff recently worked together with a team to determines the architecture of a second subcomplex of the nuclear pore complex, in so doing solving a major quandary of answering how a nuclear pore complex (NPC) can be such an effective gatekeeper, preventing much from entering the nucleus while helping to shuttle certain molecules across the nuclear envelope.

The scientific team was featured in multiple publications including Caltech and the Argonne National Laboratory Science Highlights (reproduced in part below). The research was supported in part by the Consortium, and culminated in the following publication:

Architecture of the fungal nuclear pore inner ring complex

Stuwe T, Bley CJ, Thierbach K, Petrovic S, Schilbach S, Mayo DJ, Perriches T, Rundlet EJ, Jeon YE, Collins LN, Huber FM, Lin DH, Paduch M, Koide A, Lu V, Fischer J, Hurt E, Koide S, Kossiakoff AA, Hoelz A. Science. 2015 Oct 2;350(6256):56-64. PMID: 26316600.

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Solving a Major Piece of a Cellular Mystery

This article by Argonne reproduced in part can be read here

Not just anything is allowed to enter the nucleus, the heart of eukaryotic cells where, among other things, genetic information is stored. A double membrane, called the “nuclear envelope,” serves as a wall, protecting the contents of the nucleus. Any molecules trying to enter or exit the nucleus must do so via a cellular gatekeeper known as the nuclear pore complex (NPC), or pore, which exists within the envelope.

How can the NPC be such an effective gatekeeper — preventing much from entering the nucleus while helping to shuttle certain molecules across the nuclear envelope? Scientists have been trying to figure that out for decades, at least in part because the NPC is targeted by a number of diseases, including some aggressive forms of leukemia and nervous system disorders such as a hereditary form of Lou Gehrig’s disease. Now a team of researchers from Caltech, The University of Chicago, and the Biochemistry Center of Heidelberg University (Germany), led by André Hoelz and working at three U.S. Department of Energy synchrotron light sources including the Advanced Photon Source (APS) at Argonne, has solved a crucial piece of the puzzle.

In February of this 2015, the team published a paper describing the atomic structure of the NPC’s coat nucleoporin complex, a subcomplex that forms what they now call the outer rings (see the figure). Building on that work, the team has now solved the architecture of the pore’s inner ring, a subcomplex that is central to the NPC’s ability to serve as a barrier and transport facilitator. In order to determine that architecture, which determines how the ring’s proteins interact with each other, the biochemists built up the complex in a test tube and then systematically dissected it to understand the individual interactions between components. Then they validated that this is actually how it works in vivo, in a species of fungus.

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