Biophysical Society 59th Annual Meeting Program Guide

Exhibitor Presentations Exhibit Hall C, Baltimore Convention Center

Room A: Sunday, February 8 7:30 am –9:00 am FEI Company FEI Cryo-TEM Workflow Solutions: A New Era for 3D Structural Biology A new frontier exists in unraveling interactive biological and biochemical processes and pathways at the macromolecular level. Of critical importance is the three-dimensional visualization of macromolecular structures and molecular machines in their native functional state. Three techniques play a major role in orchestrating this. Nuclear magnetic resonance (NMR) has the capability to study specific protein domains or fragments and their functional role in protein folding and dynamics and in ligand binding whereas X-Ray crystallography (XRD) allows visualizing high-resolution but more static 3D structures of apo and liganded proteins, mainly in a monomeric or dimeric state after crystal- lization. To unravel more physiologically relevant situations however, it is essential to visualize multimeric complexes in their tertiary and quaternary state and their interaction with other complexes. By performing typical cryo-TEM applications like single particle analysis or tomography, this can be achieved. In this so-called translational methodology, cryo-TEM thus provides complementary information to NMR and XRD that can be crucial for drug discovery, e.g. in terms of a better understanding of the mechanism of action inferred from the EM structure of the physiologically relevant complex. This will eventually contribute to answer real biologically as well as medically relevant questions. Latest developments in the cryo-TEM workflow have brought the 3 major structural biology technologies closer together. Now, finally, a continuum has been reached on all important aspects with regards to resolution and macromolecular scales which allows for the full deployment of the combina- tion of these technologies. Here, we will illustrate the historical context of these technologies with respect to one another and show how latest developments have reached the critical requirements to fully unleash the power of structural biology in not just answering fundamental questions, but actually contribute to curing diseases and improving health. Also, we will discuss the future of struc- tural biology based on the latest developments of the FEI workflow and its components with a special focus on the advances in contrast enhancement (phase plates) and (direct electron) detection. Presenter Chris Arthur , Applications Engineer, FEI Company

3:30 pm –5:00 pm Wyatt Technology Corporation

The Light Scattering Toolkit for Biophysical Characterization: Lab Essentials for Enhancing Studies of Purification, Crystallization, For- mulation, Conjugation, Conformation, and Interactions Biophysical techniques based on static and dynamic light scattering address many of the key analytical challenges associated with proteins, oligonucle- otides, vesicles and other biomacromolecules. This workshop covers the following topics: 1. Batch DLS—traditional cuvette-based dynamic light scattering (DLS) is a fast, easymeans of estimatingmacromolecular and nanoparticle size distributions to assess protein aggregation or the sizes of virus-like par- ticles or drug delivery nanovehicles. In microwell-plate format, DLS is a high-productivity tool useful for optimizing formulation or crystalli- zation conditions with minimal sample consumption or manual labor. 2. SEC-MALS and SEC-DLS—coupling of multi-angle static light scat- tering (MALS) and DLS detection to size-exclusion chromatography to assess molar mass, size, conformation and conjugation, in solution, independently of column calibration and non-ideal sample-column interactions. In addition to readily assessing aggregation and fragmen- tation in line with SEC purification, SEC-MALS analyzes protein conjugates such as glycoproteins or membrane proteins bound to surfactant micelles, determining protein oligomeric state and the mass of glycans, polysaccharides or surfactant modifying the protein. 3. FFF-MALS and FFF-DLS—coupling of MALS and DLS to a field- flow fractionation (FFF) device to achieve accurate characterization of macromolecules and nanoparticles from 1-1000 nm, even when solu- ble and insoluble components are both present in the solution. It does not employ a stationary phase; FFF separates without shear and with minimal surface interactions. FFF produces high-resolution size distri- butions thanks to true hydrodynamic separation upstream of the light scattering detectors. It also offers the benefits of post-separation down- stream analysis by spectroscopy for additional information on samples. 4. CG-MALS—coupling MALS to a composition-gradient device results in a uniquely powerful system for characterizing complex biomolecular interactions, label-free and immobilization-free. Because MALS measures molar masses it is one of the most useful techniques for analyzing multi-domain, multi-protein interactions that go beyond standard 1:1 interactions including systems exhibiting cooperativ- ity and allostery. CG-MALS determines the affinity and absolute molecular stoichiometry of self and/or heteroassociating systems from pM to mM. Presenter Stephanie Cope, Applications Scientist, Wyatt Technology Corporation

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Biophysical Society 59 th Annual Meeting, Baltimore, Maryland