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2022 ProgramACA2022 will include ample time for discussion and informal interactions between junior and senior scientists from all over the world, to ensure a lively exchange of ideas. Each day of the conference features a plenary lecture and parallel sessions and symposia, giving participants access to a range of topics. Each session will include several presentations relating to the session topic with approximately 40% of the topics coming from submitted abstracts. A poster competition introduces an alternative forum for interaction with the wider research community and the social program will include a welcome reception, providing an opportunity for attendees to make and renew acquaintances in a relaxed setting.
Please note that the times noted are in Pacific Time and further that this schedule is tentative and subject to change. Friday, July 29, 2022
Saturday, July 30, 2022
The application of extreme conditions enables access to exotic states of matter. Under extremes, matter undergoes drastic changes such as structural and magnetic phase transitions or exhibits rich new phenomena such as novel superconductivity. The application of extremes also enables synthesis of new exotic materials with unique characteristics. Furthermore, extremes can also be used as ‘tuning’ parameters that can be used control and understand the quantum dynamics of strongly correlated electrons. In common to these research directions is the requirement to successful apply the desired (multi-)extreme conditions as well as characterization techniques that enable in situ study of materials while under extremes. This session will address the many behaviors and phenomena that are observed under extreme conditions as well as necessary experimental and theoretical techniques. This session thus aims to bring together researchers reporting on the most recent experimental and theoretical discoveries of novel emergent phenomena as well as researchers targeting development and advancement of new techniques and approaches. Additional attention will be paid to existing and new capabilities at large-scale facilities world-wide. Finally, it will also provide a platform to exchange ideas to expand the scope of future materials research under extreme conditions
Prediction of 3D protein structure by AlphaFold2 and RoseTTAFold has achieved revolutionary accuracy using new AI methods. These programs can accurately predict the 3D structure of many proteins from 1D amino acid sequences, opening up a vast array of exciting new experiments and challenges for researchers. In this session we will explore current applications of these structures in molecular replacement, cryo-EM fitting and refinement, structure-based drug design, and tomography. We will explore what kinds of new and difficult methods have been enabled and what remains difficult. Other topics may include how error estimates on AI protein models can be incorporated into these methods, progress in modeling of protein complexes, implications of AI structions on protein design, the generation and use of structure ensembles, and new data analysis best practices that need to be developed as the use of computer-generated structures becomes more common.
Single-particle cryogenic electron microscopy (cryoEM) and tomography (cryoET) can provide remarkable insights into the structure of macromolecules in either purified form or in a cellular context, respectively. Due to advances in direct electron detector technologies and algorithm developments over the past decade, cryoEM analysis can now routinely determine structures at resolution ranges previously deemed accessible only to X-ray crystallography (2-4Å), while cryoET has moved into the sub-nanometer range. However, ultra-high-resolution structures, where individual atoms are resolved, remained only accessible by crystallographic analysis until recently. Now, with the advent of new EM hardware, including more coherent electron sources, improved energy filters and more, cryoEM analysis is able to reach atomic resolution in favorable cases. In parallel, improvement in data collection methods and reconstruction approaches has allowed cryoET to similarly break new ground, with sub-3Å reconstructions now achievable. This session highlights both the technical developments that have allowed such advances, and the biological insights facilitated by improved structural resolution obtained by both cryoEM and cryoET.
The field of microcrystal electron diffraction (MicroED) has rapidly progressed in recent years bringing exciting new opportunities to the structural biology and analytical chemistry fields. This technique has been applied to a wide range of samples, from small molecules to peptides, to soluble proteins and even membrane proteins. Several experimental protocols exist that describe the process of sequentially recording diffraction patterns from nanometer-sized crystals while the crystal is continuously rotated in a transmission electron microscope and then using these data to determine 3D structures. This session will focus on method development with emphasis on advances in sample preparation, data collection software/hardware and data processing. This session will also provide an opportunity to highlight interesting recent applications of MicroED, especially for macromolecules and membrane proteins.
TMT 3-Minute-Thesis
7/30/2022 @ 11:30:00 AM - 1:00:00 PM
Sponsoring SIG(s): YSIG Session Chair(s): Dan Decato; Kristofer Gonzalez-DeWhitt
 PL1 Etter Award:
TR2 The Role of Structural Science in Tackling a Pandemic: COVID-19 as a Paradigm7/30/2022 @ 2:00:00 PM - 5:00:00 PM Session Chair(s): Diana Tomchick
1.2.1 Structural Insights Into the Origin & Applications of Novel Properties in Quantum Materials
7/30/2022 @ 2:00:00 PM - 5:00:00 PM Sponsoring SIG(s): Neutrons/Materials/Powder Session Chair(s): Keith Taddei; Haoxiang Li 1.2.3 Beamline Automation and Autonomous Experiments (II) With the technological advancements in automation at both synchrotron beamlines and sample handling, Macromolecular Crystallography (MX) has become an indispensable method for high-resolution structure analysis of biological macromolecules. In order to tackle the most challenging projects for modern life science and drug discovery research, the developments of further automation of MX and data analysis methods using high performance computing (HPC) to derive advanced structural information from large-scale diffraction data obtained by the automation are underway. A lot of results have been obtained by automated and remote data collection even in the global movement restrictions due to the COVID-19 pandemy. In this session we will highlight the latest automated sample handling and data collection methods, techniques, and best practices for advanced data analysis from large-scale diffraction data with automation.
Powerful machine learning approaches have begun impacting cryo-EM and cryo-ET workflows in areas spanning data collection to reconstruction and model building. In many instances, these approaches are proving effective in automating labor-intensive tasks and in extracting information from the large, but low-signal datasets that electron microscopy typically produces. Additionally, careful application of these methods offers an opportunity to naturally encode prior structural information into the data analysis pipeline. When misapplied, however, the risk of introducing difficult-to-identify artifacts is significant, and robust validation methods are needed. This session features recent advances in machine learning methods and their applications to electron microscopy; highlighting the strengths, future prospects, and potential concerns of such approaches.
John Charles Howorth Spence (21 April 1946 – 28 June 2021) was Richard Snell Professor of Physics at Arizona State University and Director of Science at the National Science Foundation BioXFEL Science and Technology Center. He was endlessly fascinated by microscopy techniques and their applications in materials science (e.g. atomic-resolution electron microscopy and its use for the study of atomic defects in crystals and semiconductors) and molecular biology (e.g. x-ray imaging and crystallography techniques for imaging protein dynamics). He was a world-class inventor who tirelessly pursued truly unique and original ideas. He supported and inspired countless students, postdocs and colleagues along the way. Among many accolades, he was a Fellow of the National Academy of Inventors, honorary Fellow of the Royal Microscopical Society, Foreign Member of the Royal Society, and was awarded the Gregori Aminoff Prize in 2021. John's interests extend to music, literature, book-writing, flying, and sailing. He was an accomplished player of the piano, guitar and the flute and has been involved in many bands throughout the years. His most recent books published include "Lightspeed: The Ghostly Aether and the Race to Measure the Speed of Light" and "Spitfire Pilot Lou Spence: A Story of Bravery, Leadership and Love". Talks in this symposium will focus on various aspects of John's later years of work related to XFEL science and his pioneering contributions to the development of Serial Femtosecond Crystallography (see also the related symposium dedicated to John Spence at M&M - P12 on this website: https://www.microscopy.org/MandM/2022/program/descriptions.cfm.
Sunday, July 31, 20222.1.1 New Developments for Operando and In Situ Diffraction Rational design of new functional solid state materials requires an atomistic understanding of reaction mechanisms during synthesis. To optimize the performance of these functional materials, monitoring the structural evolution of materials during device operation is key. In situ and operando X-ray/neutron diffraction have emerged as one of the most important characterization tools to study these chemical processes. The tremendous advancements of X-ray and neutron sources in recent years, together with improved instrument design, data acquisition and analysis enabled the unprecedent speed of diffraction data collection, on-the-fly data analysis and quantitative structure analysis of large amounts of data sets. Thus, we feel it is timely and imperative to highlight some of these exciting progresses and provide a platform to exchange ideas about future directions. This symposium invites contributions from technique/instrumentation developments, advanced data analysis and scientific applications for operando and in situ X-ray/neutron diffraction.
The Covid-19 pandemic and the lockdowns and travel bans enforced over the world have had a big impact in access to large scale experimental facilities, which needed to adapt the way of operation drastically. As a result, many efforts started at various beamlines to develop complex infrastructure for remote experiments. The "Remote Access" session will discuss some of the new protocols, equipment, and also interfaces set up to provide users mail-in or remote services. The impact on the future experimental development and interaction with the users will be examined under various aspects, such as enabling new research approaches by automation or the opportunities for diversity, equity, and inclusion as well as economic justice.
Modern protein structures are based nearly exclusively on data collected at cryogenic temperatures. With the cooling process being thought to introduce bias in the functional interpretation of structural results. Structure solution at near physiological conditions can reveal previously hidden structural ensembles in macromolecular structures. Studying room-temperature conformational ensembles using crystallography, NMR, or small angle scattering can reveal motions crucial for catalysis, ligand binding, and allosteric regulation. This session will focus on insights gained from the study of macromolecules at or near physiological conditions.
This session aims to trace the advance of the methodologies used in structure analysis in terms of the techniques applied by different generations of crystallographers. This will provide a context for the historical development of the technology, techniques, and practices used today. The past high level of technical involvement by the user, and the desire to perfect the results as much as possible have abated, with the advent of automated rapid-throughput analyses accompanied by computer-controlled validation. At the same time, non-routine or previously unfeasible results, involving e.g., twinning, modulation, or ab-initio powder diffraction analysis, can be undertaken today with a reasonable expectation of success. This evolution of techniques and tools has also had a strong impact on the user's educational point of view. It transformed the emphasis from technical acuity with instrumentation, software, and fundamental crystallography itself, to a stronger focus on the results and their implications in a broader scientific context. Submissions are welcome from all experience levels.
PL2 Trueblood AwardArlie McCoy
7/31/2022 @ 1:00:00 PM - 2:00:00 PM
Advances in computational power have afforded the expansion of machine learning (ML) into many aspects of research. Complementing sessions on ML in Crystallographic structure solution and CryoEM, this session will provide a forum for other applications of interest to our field, from small molecule and biomacromolecular techniques to automation of routine tasks. Topics (to be confirmed) include crystal screening, RNA structure prediction, small molecule/drug design and others to be identified from submitted abstracts Invited Speakers:
This session will highlight the application of structural biology to understand host–pathogen interfaces. Examined topics may include, but are not limited to, structural studies on viral, bacterial, and fungal proteins, as well as proteins mediating host-pathogen interactions of eukaryotic and protozoan parasites, with a focus on their functional mechanisms or interactions with host cell metabolites, receptors, and antibodies. Structure-based vaccine design and antibody engineering studies are also welcome. Research aiming to combat infectious diseases by using structural biology methods such as cryo-EM, X-ray crystallography and integrated or complementary techniques will be presented.
When is a structure too poor to publish? How much should scientific impact affect this decision? What are some recommended procedures for publishing poor quality structures? What compromises are involved in the publication of "low quality" structures? If you have ever asked yourself these questions, then share your insights, structures and problems with the small molecule community. This is a great opportunity for young crystallographers to share their work, where they can interact with a friendly audience, who with years of experience will provide constructive advice. Problems might include charge imbalance or other chemical issues, poor resolution or data completeness, complicated disorder, highly restrained models, unexplained residual electron density, etc. Talks in this session will be restricted to approximately 5 minutes in order to encourage audience participation and discussion. All talks will be selected from submitted abstracts. Those who submit abstracts to this session may still submit a second abstract to other sessions at no additional fee.
Monday, August 1, 20223.1.1 Frontiers Of Local Structure Analysis: Total Scattering, Single-Crystal Diffuse Scattering & More As our ability to investigate and understand crystal structures has improved, we have increasingly seen the importance of locally-correlated structures within well-ordered materials. Observing local structure via pair distribution function (PDF) measurement in powders or with single crystal diffuse scattering has become increasingly accessible, with improvements in both instrumentation and computing allowing for more comprehensive and detailed measurements and more complete and better-guided analysis. In this session, we will show examples of powder-based PDF studies and single crystal diffuse scattering and how each can help determine local structures within crystalline materials and reveal structure-property relationships that were previously overlooked. Contributions on the aforementioned two topics from both X-ray and neutron areas are welcome.
3.1.2 Home-Built Software & Hardware
8/1/2022 @ 8:30:00 AM - 11:30:00 AM The changing role of home-built software and hardware is the theme of this half-day session. Purpose-built in-house software for crystallography has spanned the entire range of uses, from specific tasks such as data format-changing to more global data- and structure-analysis packages. Crystallographic software has a singular characteristic in that a large fraction of published crystallographic results are obtained using software that originated in active crystallography laboratories. Less famous are applications prepared locally to improve work flow and data security. Similarly, hardware ranging from simple gadgets for crystal handling and mounting all the way to diffractometers for use with unique radiation sources have been custom-made for crystallographic applications. The conditioning of sample environments, including the creation of extreme conditions, has been an area of active development, as has the development of systems for diffraction under in situ conditions. This session will welcome contributions from all who create and/or adapt software or hardware for crystallographic use. Innovative applications for any diffraction experiment in the home laboratory, at a synchrotron or a neutron source may be presented. As in the previous editions of this topic, contributions of a historical nature will be welcome.
Protein-nucleic acid complexes regulate gene expression in hosts and pathogens. The 3D structural underpinnings of these key macromolecular machines are critical for understanding gene regulation by numerous pathways and to define potential pharmaceutical targets. This session will present cutting-edge research on protein-RNA and protein-DNA structures, with emphasis on noncoding RNAs, post-transcriptional modifications, and new insights from cryo-electron microscopy.
Crystallographic education is vital to every aspect of our profession from the training of current and next generation scientists to the potential for shaping public perceptions. This session offers an informal platform for speakers to communicate their approaches and techniques that promote the learning process of crystallography. The short format of this session (10 minute talks) will encourage speakers and attendees to freely share ideas on focused topics that range from innovative hands-on exercises, virtual resources, and novel must-have classroom modules.
3.1.5 Scanning Imaging & Tomography Based on Scattering Contrast
8/1/2022 @ 8:30:00 AM - 11:30:00 AM
Sponsoring SIG(s): Small Angle Scattering
Session Chair(s): Lin Yang; Masa Fukuto
Brief Session Description: In scattering measurements on complex structures such as biological tissues and fabricated devices, all structural components within the illuminated volume contribute to the observed scattering intensity. With a small x-ray beam as the probe, raster scanning can be used as an imaging technique to map out the distribution of these structural components. Tomographic data collection is also possible to resolve structural distributions in 3D. This session is intended to inform the community of the current research examples, in hope of inspiring wider application and further development (e.g. the use of computation and machine learning to distinguish different structural components) of this technique.
PL3 Bau Neutron Diffraction AwardArthur J. Schultz
8/1/2022 @ 1:00:00 PM - 2:00:00 PM
3.2.1 Educating The New Generation Of Users Many facilities run courses to educate the next generation of users and pass on tips, tricks, and new developments. These span a wide range of areas and techniques. From a source perspective, they include synchrotron, neutron, and cryo-EM facilities. From a technical perspective, there are courses that focus on whole areas of structural biology and specific techniques. In this session, we invite organizers of these courses to describe best practices for educating the community, and the impact they are making on the next generation of users. We encourage a snapshot of the training to be provided and aim to serve as a forum to advertise these workshops and courses, publicizing them to the community. 3.2.2 Fragment Based Drug Discovery Fragment Based Drug Discovery (FBDD) utilizes small molecule compounds to help identify starting points in the drug discovery process. This process allowed for the discovery of lead compounds for difficult protein targets with small/shallow pockets or protein-protein interactions. In contrast to other screening techniques such as High-Throughput Screening (HTS) or DNA-encoded Libraries (DEL), FBDD utilizes small libraries of molecules (< 2000) with molecular weights less than ~200 Da. FBDD has been key in the development of multiple approved drugs and dozens of other drugs in clinical trials. This session will focus on the biophysical and structural techniques used in FBDD to identify initial starting points, optimization by fragment growing/linking, and the route to lead optimization.
Structural biology to date has mostly been described using static snapshots of macromolecules. Recent developments in new sources, sample preparation techniques, and software developments have enabled researchers to probe time-resolved structural dynamics of macromolecules from the ultrafast femtosecond time-scales up to milliseconds or longer. These developments allow chemically and functionally biological intermediates to be studied with unprecedented spatial and temporal resolution. Similarly, there have been developments that allow probing components within complex systems undergoing structural changes during biochemical and biotechnological processes. This session aims to cover the latest developments in the field of time-resolved structural dynamics and kinetic processes from a variety of techniques using X-ray, neutron, or electron sources in solution or in crystals.
A push-button automation approach to crystal structure determination by X-ray diffraction is all very well for the vendors and for inexperienced users, but a practicing crystallographer is likely to encounter samples requiring a better grasp of the underlying theory, instrumentation, and software to understand what's happening, to interpret the results sensibly, and to know what to do when the automatic methods don't deliver the goods. In this session we seek to prise open some of the popular 'black boxes' and reveal what's inside, so that an informed user has some idea how to tinker around with the controls and maybe even rewire some of the inner workings. We hope to have access to insider knowledge about procedures such as the automatic derivation of unit cells from initial diffraction images, the choice of space groups, how structures are determined by charge flipping and dual-space approaches, and how constraints, restraints and other refinement tricks and tools work.
This session will be comprised of talks describing exciting new macromolecular structures. Talks focusing on structures will be highlighted from across all disciplines of structural biology (Cryo-EM, X-ray Crystallography, NMR, SAXS, etc.). The majority of the talks will be selected from submitted abstracts
Structural biology researchers now access light sources and electron microscope facilities almost exclusively from remote locations due to the pandemic. This is expected to continue in the future. As a result, more users are exposed to different facilities and their varied interfaces and methods. The upcoming APS shutdown will further increase crystallographers' mobility in the US. In electron microscopy the field is rapidly evolving, and in crystallography, new and renewed crystallographic methods like serial crystallography, room temperature data-collection, and machine learning further contribute to a variable synchrotron environment. This is a great time for finding standards and collaboration opportunities, to improve the users’ experience and scientific output, and best use staff and facility resources. From the wetlab, over beamlines and microscopes, to data processing and depositing final results, this is a wide field. We invite contributions from facilities, academia and industry that provide an overview of standardization possibilities in the different areas, with the speakers not talking exclusively about their own work. This session aims to foster collaboration between facilities and to discuss new standards and compatibility between existing solutions - with the goal to allow researchers to collect better data and focus on their science rather than technicalities.
Recent advances in light sources, experimental methods and computational algorithms have enabled exciting new discoveries using small angle scattering (SAS). This session is devoted to discussing the latest advances in methods and applications of X-ray and neutron SAS. The primary aim is to bring together cutting-edge advances utilizing SAS on both soft matter and biological systems, including time-resolved studies, contrast matching, dynamic and flexible systems, hybrid modeling, novel experimental apparatus and methods, and new computational approaches. This session will reflect the state of the art in SAS methods.
Chemical structure, whether it be molecular or crystallographic, is an inherently three-dimensional property that is most often displayed on two-dimensional surfaces, such as printed images or computer screens. Advancements in visualization technology have created new ways for scientists to present dynamic processes and structural data in engaging and helpful formats. This session focuses on communicating science through visualization using the latest developments in 2D and 3D methods. This includes, but is not limited to, animation and rendering techniques, lighting and coloring effects, VR, AR, and 3D printing, and other advanced display methods used by structural scientists to visualize molecular interactions, reactions, protein structures, crystal structures, and crystallography principles, or to aid in structure-based drug design. 4.1.5 Cool Structures I 8/2/2022 @ 8:30:00 AM - 11:30:00 AM Structure elucidation from nanometer-sized crystals has positioned microcrystal electron diffraction at the forefront of structural science. This session will feature small molecule (< 150 atoms per molecule) structures solved using MicroED and aims to highlight successes made possible by MicroED. Speakers will be selected from contributed abstracts. Submissions from students are encouraged.
PL4 Fankuchen AwardDavid S. Goodsell
8/2/2022 @ 1:00:00 PM - 2:00:00 PM
This session will discuss recent advances in both xfel and synchrotron serial crystallography resulting from improvements in beamlines, detectors, data collection strategies, software and computational resources.
Many biological systems need to be studied at relatively high concentration, such as intrinsically disordered proteins and biomacromolecules in the pharmaceutical products. The discovery that liquid-liquid phase-separation (LLPS) plays a vital role in human disease has stimulated much recent research into the phase properties of concentrated solutions of biomolecules. Remarkably, it is now understood that the structural biology of proteins with intrinsically disordered regions (IDPs) is central to understanding this phenomenon. In parallel, the self-association, rheological properties and solubility limits of concentrated biologics, particularly monoclonal antibodies (mAbs), continues to be a subject of great practical importance in pharmaceuticals. The conventional use of dilute solutions by small angle scattering has already yielded important insights into the conformational changes that are associated with aggregation and LLPS behavior. Monoclonal antibody studies, on the other hand, have focused on interpreting structure factors from concentrated solutions to gain insight into intermolecular interactions. Simulations inspired by advances in Soft Materials, Colloid Science, and active matter have also played an important role in this field by incorporating ever more sophisticated particle models. This session seeks to bring together experts in this wide range of fields having common interest in concentrated or phase-separated biomolecular solutions.
4.2.3 Cool Structures II Structure elucidation from nanometer-sized crystals has positioned microcrystal electron diffraction at the forefront of structural science. This session will feature small molecule (< 150 atoms per molecule) structures solved using MicroED and aims to highlight successes made possible by MicroED. Speakers will be selected from contributed abstracts. Submissions from students are encouraged.
4.2.4 General Interest 2
Structural cell biology has dramatically advanced from studying individual proteins and enzymes to macromolecular assemblies of sizes with an increasing complexity–doubling about every decade over the last century. With the introduction of direct detectors, cryo-electron microscopy (cryoEM) was revolutionized and established a methodology to study massive biological assemblies that are recalcitrant to crystallization, at resolutions previously only attainable by X-ray crystallography. Moreover, focused-ion beam (FIB) milling and cryo-electron tomography (cryo-ET) now allow for the visualization of macromolecular machineries in their native cellular environments. The combination of these structural methods with improvements in traditional reconstitution biochemistry and cross-linking mass spectrometry enabled structural advances that seemed impossible less than a decade ago. In this session titled, “Structures of Very Large Assemblies”, we celebrate some of the recent spectacular advances – pushing the boundaries of larger and more complex cellular machineries, which remains a major frontier.
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