Challenges in biological cryo electron microscopy: Faraday Discussion

13 - 15 July 2022, Sheffield, United Kingdom


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Introduction

This Faraday discussion will be a hybrid event, allowing participation both in person and online. 

Welcome

Join us in Sheffield, or online, in July 2022 for this addition to our Faraday Discussion series. For over 100 years and 300 meetings, Faraday Discussions have led the conversation on the study of the sciences lying between chemistry, physics and biology. Many of these Discussions have become landmark meetings in their field with the unique format allowing for in-depth discussions and opportunities to establish new collaborations.
 
This Discussion is for established and early-career scientists, post-graduate students and industrial researchers interested in the expanding field of cryo-electron microscopy. Researchers in this area who based in cryo-EM facilities or research institutes, or in departments of biology, chemistry, structural biology, virology, cell biology, molecular biology or biophysics etc are all welcome. Oral and poster presentation opportunities are available to all these groups, and we invite you to submit an oral or poster abstract and join us to make your contribution alongside leaders in the field. 

The Discussion will bring together expertise from the UK and the international cryo-electron microscopy community to discuss current developments and new challenges. 
 
On behalf of the organising committee, I look forward to welcoming you to Sheffield, or if you are joining us virtually, online.
 
Stephen Muench
Chair

Format

Faraday Discussions remain amongst the only conferences to distribute the speakers’ research papers in advance, allowing the majority of each meeting to be devoted to discussion in which all delegates can participate.  Following each meeting a written record of the discussion is published alongside the papers in the Faraday Discussions journal.

Find out more about the Faraday Discussions in the video available. 


Themes

Cryo-electron microscopy has undergone significant developments in microscope design, camera technology and data processing regimes, but there are significant challenges that remain and opportunities to explore, many of which must be tackled by the community as a whole rather than by individual groups. This meeting will bring together expertise from both these centres and the international cryo-EM community to discuss the current developments and challenges

This Faraday Discussion will be organised into the following themes:
 
Sample preparation in single particle cryo-EM
Sample preparation is central to electron microscopy and is currently a significant bottleneck in many experiments. There are currently a number of limitations in our fundamental understanding of the sample preparation process, in particular the way a protein sample interacts with a grid support and how this affects the sample’s integrity.  The surface chemistry of these grids is poorly characterized. Discussion in this section will focus on dealing with the air/water interface, improving sample reproducibility and changing the chemistry of support grids to better facilitate sample preparation.
 
Pushing the limits in single particle cryo-EM
Despite the recent massive improvements in single particle cryo-EM, obtaining sub-2Å structural information is still a major challenge. There are a number of limitations that hinder our ability to obtain atomic resolution maps, including imaging conditions and data processing approaches. In this section, we will discuss what factors currently limit the resolution of most structures, and how we can quickly screen buffer conditions to optimise data quality, improve the signal-to-noise within data, accurately correct for factors such as magnification anisotropy and Ewald sphere curvature and improve current methodologies for identifying different conformational states. This session will also discuss the latest advances in phase plate technology and opportunities for further developments.
 
Tomographic analysis, CLEM
Many structural techniques can give atomic or near atomic level information, but many lack the ability to study proteins within a near native environment, for example within its cellular compartment. However, tomographic analysis provides both high resolution and the ability to work within the cell. With advances in labelling technologies and better stages it is now possible to conduct correlative electron microscopy (CLEM) analysis which can localise labelled proteins within the cell to high precision. This session will discuss the challenges facing this developing technology and how the community can address them. Key discussion points will be how we can build better sample stages, labelling technologies and tilt collection strategies, and if improved grid chemistry could help with sample preparation.
 
Map/model validation and machine learning in EM
Developments in cryo-EM are creating new opportunities within structural biology, however there are significant problems with ensuring the integrity of the field in terms of dealing with inherently low signal-to-noise images. Unfortunately, there have been recent examples in the literature of poorly refined and validated structures from cryo-EM data and with the rapid expansion of EM facilities throughout the UK and worldwide, how do we ensure that sufficient tools and training are provided to maintain high standards of model validation? Moreover, what role will the implementation of more machine learning approaches play in cryo-EM data processing and validation? In this session, we will discuss how we can ensure cryo-EM derived maps are validated, the current tools for model building and how they can be improved, and the role of ever changing data processing approaches.  
Speakers
Helen Saibil (Introductory Lecturer), Birkbeck, University of London, United Kingdom

Helen Saibil is a structural biologist at Birkbeck, University of London, where she built up a cryo electron microscopy lab. She was educated at McGill University, Montreal, and at Kings College London. Her research career started at Kings, then the Centre d'Etudes Nucléaires, Grenoble, and Oxford University, before settling at Birkbeck. Her research is on macromolecular machines, both in vitro and in their cellular context. A major focus is the action of molecular chaperones in assisting protein folding, unfolding and disaggregation. In addition, she studies the actions of intracellular pathogens and pore forming toxins on host membranes.


Werner Kühlbrandt (Closing Remarks), Max Planck Institute of Biophysics, Germany

Werner Kühlbrandt studied chemistry and crystallography at the Free University Berlin, and biochemistry and biophysics at King’s College London. He did his PhD with Nigel Unwin at the MRC Laboratory of Molecular Biology in Cambridge, UK, investigating the structure of two-dimensional ribosome crystals by electron microscopy. As a postdoc, he turned to investigating the structure of membrane proteins, first at the ETH Zürich, and then at Imperial College London. As a research group leader at EMBL Heidelberg he determined the high-resolution structure of the plant light-harvesting complex LHC-II by cryoEM. Since 1997 he has been a director at the Max Planck Institute of Biophysics in Frankfurt, Germany, where his department of Structural Biology studies large membrane protein complexes primarily by single-particle cryoEM and electron cryo-tomography.
 


Thomas Braun, University of Basel, Switzerland

Thomas Braun studied biophysics at the Biozentrum of the University Basel, Switzerland, and completed his PhD 2002 on high-resolution electron microscopy of membrane protein channels and transporters. In his postdoc and senior researcher at the Physics Institute of Basel and the Trinity College Dublin (Ireland), he developed nanomechanical sensors for real-time analysis of biological processes. 2009 he returned to Basel to the Center of Cellular Imaging and Nanoanalytics (C-CINA) and now leads a research team at the Biozentrum of the University Basel. His group focuses on developing novel microfluidic sample-preparation methods for protein isolation, high-resolution electron microscopy, and “single-cell visual proteomics.”
 


Daniel Clare, Electron Bio-Imaging Centre, Diamond Light Source, United Kingdom

I completed my PhD in Structural Biology, at the laboratory of Professor Helen Saibil in Birkbeck College, London. During my PhD I focused on membrane protein structure determination using 2D crystallography and cryo-EM. However the lack of crystalline order necessitated the application of single particle averaging methods and this work was performed in collaboration with Elena Orlova. After my PhD I continued to work in Professor Saibil’s laboratory but switched entirely to single particle analysis and applied cryo-EM to molecular chaperones to elucidated some of the first substrate bound and ATP triggered structures of GroEL. In 2015 I moved to Diamond Light Source to set up and co-manage the new national cryo-electron microscopy facility, eBIC. Currently the facility comprises seven state-of-the art cryo-electron microscopes, four of which are running full internationally recognised external user programs. Data collected at eBIC, using a free-at-the point of access model, has been crucial in number of high impact publications from UK and European based scientists. During my time at Diamond I have maintained my research interests predominantly working on the chlamydia infection of mammalian cells using cryo-FIB milling and electron tomography. I currently have a joint PDRA with the membrane protein lab at Diamond looking at optimising membrane protein structure determination by cryo-EM. As well as this I am involved in a number of collaborations with Rosalind Franklin institute and industrial partners looking at the next generation cryo-EM and freezing devices.


Chris Russo, Laboratory of Molecular Biology - MRC , United Kingdom

Born in Detroit Michigan, Chris attended the University of Notre Dame where he studied electrical engineering and philosophy. He then went on to graduate school at Harvard and MIT, where he studied physics and medicine under the supervision of Jene Golovchenko (Physics, Engineering) and Daniel Branton (Biology). During this time, he developed a new technique to create nanopores in graphene with atomic precision that combined ion bombardment with high energy electron irradiation.

He then moved to the MRC Laboratory of Molecular Biology in Cambridge, UK, to work on developing new methods for electron cryomicroscopy (cryo-EM). Chris has since started his own group at LMB, and continues to study the physical phenomena that limit resolution in cryo-EM and thus enable the development of new devices, instruments and methods to improve the imaging power of the electron microscope in biology.


Sjors Scheres , MRC Laboratory of Molecular Biology, United Kingdom

Sjors studied chemistry at Utrecht University, The Netherlands, where he also obtained his PhD in protein crystallography. He was a post-doc in the group of Jose-Maria Carazo in Madrid, before he started his group at the LMB in 2010. Since 2018, Sjors is also joint Head of the Structural Studies division. His main interests lie in the development of new methods for high-resolution cryo-EM structure determination, and their application to amyloid filaments. Sjors is the main author of the RELION program for cryo-EM structure determination, and he solved numerous structures of amyloid filaments, among others of the proteins tau, alpha-synuclein and amyloid-beta.


Rebecca Thompson, University of Leeds, United Kingdom

Rebecca is the Head of Faculty Biological Sciences Research Facilities and Deputy Director Asbury Biostructure Laboratory, University of Leeds. In this role she oversees delivery of range of research facilities, including cryo-electron microscopy capabilities with two state-of-the-art Titan Krios microscopes. Her current research interests span cryo-electron microscopy and include developing and optimising workflows for high resolution structure determination of macromolecular complexes by single particle analysis and using cryo-electron microscopy to image protein:membrane interactions. 
 


Giulia Zanetti, Birkbeck, University of London, United Kingdom

After undergraduate studies in Italy and Australia, Giulia completed her PhD in Oxford (2004-2009), working on cryo-tomography studies of viral glycoproteins. After a postdoc at the University of California, Berkeley, she joined the Institute of Structural and Molecular Biology (ISMB) at Birkbeck College in London. In 2014 Giulia was awarded a Dorothy Hodgkin Royal Society fellowship, which kick-started her lab. Currently her group is pushing the boundaries of cryo-tomography to understand mechanisms of complex membrane trafficking processes. Integration with biochemical techniques and collaboration with labs who use complementary approaches is helping to understand how the COPII coat remodels membrane and how this process is regulated. 


  • Andrea Thorn University of Hamburg, Germany

Abstract Submission

Oral Abstracts 

Oral abstract submission and paper submission are now closed. 

A full research paper always accompanies oral presentations at Faraday Discussions. The research papers are reviewed upon submission and are sent to all delegates 4 weeks before the meeting so they can be read in advance. At the meeting the presenting author is allowed five minutes to highlight the main points of their paper, and the rest of the time is for discussion. The discussion is recorded and will be published alongside the research paper in the Faraday Discussion journal.  

Poster Abstracts - deadline extended until 23 May

Submit your poster abstract by 23 May 2022. Posters are displayed throughout the meeting, both in-person and virtually. The Faraday Division Poster Prize will be awarded to the best poster presented by a student.
 
As this Discussion is being planned as a hybrid event we will be using a dedicated online poster platform to show all posters. Poster presenters who are attending the Discussion in-person will also need to print and display their poster physically. If your poster is accepted for this event, you will receive an email from us with further information for those attending in-person and inviting you log on to the poster platform where you will be able to upload a PDF of your poster.

Additional Information

All oral and poster abstracts will be reviewed. Authors will be notified of the outcome of the review process within about 6 weeks of the submission deadline. The abstracts should be no longer than one A4 page in portrait layout. Please ensure you provide the details of the presenting author and indicate whether you are submitting an abstract for oral or poster presentation. 

Registration

Planning your trip

We encourage delegates who are planning to attend events in person to arrange suitable travel and accommodation insurance, which should include cover for the postponement or cancellation of travel caused by regulations and guidelines relating to Covid-19. We also recommend considering flexible travel and accommodation booking options where possible.

In-person registration includes:
  • Attendance at all scientific sessions
  • Live interaction with delegates attending virtually
  • Attendance at the poster session and access to the virtual poster gallery
  • Refreshments throughout the meeting and lunch on all three days
  • Attendance at the poster drinks reception on 13 July
  • Attendance at the conference dinner on 14 July
  • Access to all journal paper pdf “pre-prints” before the meeting
  • Access to recordings of all scientific sessions post-event
  • ***A copy of the Faraday Discussion journal volume, issued approximately 5 months after the meeting, containing all papers presented at the meeting and accompanying discussion comments.
Virtual registration includes:
  • ​Attendance at all scientific sessions via the Royal Society of Chemistry’s virtual conference platform
  • Live interaction with delegates attending in-person and other virtual delegates
  • Access to the virtual poster gallery and exhibitor/sponsor virtual rooms
  • Access to all journal paper pdf “pre-prints” before the meeting
  • Access to recordings of all scientific sessions post-event
  • ***A copy of the Faraday Discussion journal volume, issued approximately 5 months after the meeting, containing all papers presented at the meeting and accompanying discussion comments.
In-person registration fees are as follows (subject to VAT at the prevailling rate):
 
Type Early bird Standard
RSC member* £315 £365
Non-member** £415 £465
Student RSC member* £145 £195
Student non-member £175 £225
Accompanying persons £100 £100

Please note accommodation is not included in the in-person registration fee. 

Virtual registration fees are as follows (subject to VAT at the prevailing rate):
 
Type Cost
RSC member* £95
Non-member** £145
Student RSC member* £45
Student non-member £65

* If you are a Royal Society of Chemistry member and wish to register for this meeting, please select the member option on the online registration page. You will need to enter your membership number.

**For non-member registrants, affiliate membership of the Royal Society of Chemistry until the end of June 2023 is available, the affiliate membership application will be processed and commence once the registrant has attended the event.
 
***Excluding students, who can order the volume at a reduced price at the conference. 

Student Delegates 

In order to encourage undergraduate or postgraduate students to attend the Discussion, a reduced conference fee is available for students. This fee applies to those undertaking a full-time course for a recognised degree or a diploma at a university or equivalent institution.

A copy of the Faraday Discussion journal volume containing papers presented at the Discussion (issued approximately 5 months after the meeting) is not included in the student registration fee. Students may purchase a copy of the volume at less than half price. This discounted price is available to delegates when ordering during the registration process, or orders placed at the meeting where an application form will be made available.  

Accompanying person

If you would like to bring a guest to the conference, this can be done during the registration process. There will be a charge of £100 which will include all lunches, refreshments and the conference dinner. The fee does not include attendance at any scientific sessions, journal paper pre-prints or the journal volume.

Accessibility 

The Royal Society of Chemistry is keen to encourage and enable as many people as possible to attend our events, to benefit from the networking opportunities and the chance to hear talks from leaders in the field. If you would like to discuss accessibility, please contact us to discuss your requirements so that we can enable your attendance.
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If you are an RSC member and a PhD student or postdoctoral researcher based at a higher education or research institution you are eligible to apply for a Researcher Development Grant.

This grant can provide up to £500 towards activities that will develop your skills and experience as a researcher, which includes participation at conferences, either in-person or virtual.

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You can apply for up to a maximum of £1000/year to assist with additional financial costs that you incur for care usually provided by you whilst you attend a chemistry related meeting, conference or workshop or a professional development event.

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You are eligible to apply if: 
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Sponsorship & supporting organisations
A selection of sponsorship opportunities is available for companies who would like to promote their activities at the 2022 Faraday Discussion series

There are opportunities available to become the Faraday Discussion series sponsor,  Research & Development partner or Poster prize series sponsor as well as some individual meeting options. A sponsorship menu document is available to download from this page with more details and prices.

Please note that exhibition spaces are limited, spaces will be allocated on a first come first served basis.

If you would like more information about sponsoring the 2022 Faraday Discussion series, please contact the Commercial Sales Department at the Royal Society of Chemistry on advertising@rsc.org. Sponsorship Menu
Venue
The University of Sheffield

The Edge, The University of Sheffield, The University of Sheffield, Endcliffe Village, 34 Endcliffe Crescent, Sheffield, S10 3ED, United Kingdom


This event is a hybrid event. For those attending in-person, venue details are as above. Virtual attendance will take place via the Royal Society of Chemistry’s virtual conference platform. For details of what’s included in virtual and in-person attendance, please see the registration section.
 
We are actively planning to hold this event in a hybrid format. Should the event move to be held in virtual-only format, any in-person delegate registrations will be refunded for the difference between in-person and virtual registration fees.
Accommodation
There are 2 hotels on the Endcliffe Campus that are a short walk from The Edge Conference Centre.  These need to be booked and paid for directly with the hotel.  There are a small number of rooms at each venue allocated to the event, please quote KX66869.  You will need to call to secure a room.

Jonas Hotel Please call 0114 222 8816 and quote KX66869 to get a room, these rooms are not available to book on line. https://www.jonashotel.co.uk/ £45-55

Halifax Hotel Please call 0114 222 8810 quote KX66869 to get a room, these rooms are not available to book on line. https://www.halifaxhall.co.uk/

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