215
Biophysical Society 58
th
Annual Meeting, San Francisco, California
5:00 pm–6:30 pm
Asylum Research, an Oxford Instruments Company
New blueDrive™ Photothermal Excitation for Superior AFM
Tapping Mode Imaging
Asylum Research, an Oxford Instruments company, will introduce its
new blueDrive Photothermal Excitation capabilities exclusively available
on Cypher™, the highest resolution fast scanning AFM. blueDrive sig-
nificantly enhances the performance of tapping mode imaging with more
simple, stable and quantitative operation, and providing extremely clean
tunes in both air and water. Typically, a piezoacoustic excitation has been
used to drive the cantilever oscillation. Though piezo drive is favored for
design simplicity, the response of the cantilever is often far from ideal, caus-
ing users to spend countless time selecting a clean cantilever tune. Asylum’s
blueDrive excitation mechanism produces an almost perfect response by
directly exciting the cantilever photothermally with a blue laser. blueDrive
is ideal for high resolution imaging of biological samples in fluid includ-
ing proteins, lipids and nucleic acids, as well as force measurements and
nanomechanics. In this presentation, we will explain how blueDrive works,
how it achieves simple cantilever tunes, and show real world results for
biophysics applications.
Presenter
Nick Geisse, Applications Scientist, Asylum Research, an Oxford
Instruments Company
7:00 pm–8:30 pm
FEI Company
Cryo-TEM: ANewEra for 3DStructural Analysis of ProteinComplexes
A new frontier exists in unraveling interactive biological and bio-
chemical processes and pathways at the macromolecular level. Of criti-
cal importance is the three-dimensional visualization of macromo-
lecular structures and molecular machines in their native function-
al 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 crystallization. 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 understand-
ing 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
three 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 combination 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
structural biology based on the latest developments of the FEI workflow
and its components.
Presenters
Marc Storms, Marketing Manager, Life Sciences, FEI Company
Jeff Lengyel, Product Marketing Manager, FEI Company
Eric Hnath, Product Marketing Manager, Structural Biology, FEI Company
Thomas Wohlfarth, Director, Structural Biology Businesses, FEI Company
Monday, February 17
8:00 am–8:45 am
FEI Company
A Fully Automated Imaging System for Correlative Light and Electron
Microscopy
See page 66 for session description.
Presenters
Alex de Marco, Product Marketing Manager, FEI Munich GmbH
Gregor Heiss, Product Marketing Engineer, FEI Munich GmbH
Liesbeth Hekking, Applications Development Engineer, FEI Company
Matthias Langhorst, Segment Director of Cell Biology Solutions,
FEI Company
9:00am–10:30am
Park Systems, Inc.
New Door to Live Single Cell Research
Atomic Force Microscopy (AFM) is a powerful measurement technique
for nanoscale science. AFM is able to provide high-resolution imaging
of biological structures below the optical limit as well as the monitoring
of the dynamics in biological systems and processes under physiological
conditions; however, certain limitations for AFM still exist in the field
of bio-applications. In recent times, the development of another kind
of scanning probe microscopy (SPM) technique, scanning ion conduc-
tance microscopy (SICM), has overcome these limitations and enabled
noninvasive, nanoscale investigation of live cells. SICM applications
include imaging of cell topography, monitoring of live cell dynamics,
mechanical stimulation of live cells, surface patterning, and so forth.
We at Park Systems have developed AFM for advanced nanoscale metrol-
ogy, which separates the z-scanner from the x-y scanner. An independent
z-scanner also provides an excellent platform for developing other SPM
techniques such as SICM. In addition, the platform which separates the
z-scanner from x-y scanner, enables us to easily switch between an AFM and
an SICM z-scanner to apply both techniques without moving samples. The
common glass micropipette is used in SICM as the sensitive probe, instead
of a silicon-based stylus, and can glide over live cells while maintaining an
absolute non-contact imaging mode. Its electrochemical current feedback
system further enhances biological sample imaging. Combining confocal
fluorescence data to the SICM3D data, using an image overlay feature, pro-
vides even more data about structure of cells as related to their membranes.
