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The goal of the NYSBC cryoelectron microscopy facility is to help
researchers elucidate the intermolecular interactions and domain
architectures of macromolecules within their native cellular
assemblies. Towards this goal, the facility has brought together a
combination of instrumentation and staff expertise that supports the
determination three-dimensional structures using the four major
techniques available to the field:
A. Electron crystallography
B. Helical reconstruction
C. Single particle analysis
D. Electron tomography
The first three techniques are applicable to samples that can be
biochemically isolated; these samples require high purity as well as a
high degree of structural homogeneity. These are the techniques that
produce the highest resolution, which can approach atomic resolution
in favorable cases. Fitting atomic models to the resulting structures
is a common approach for interpreting the resulting structures and
deducing interactions between domains or subunits of a larger
assembly. Electron tomography, in contrast, can be used to visualize
highly-complex and heterogeneous samples, such as tissue sections, or
pleomorphic assemblies such as liposomes. Since there is often no aid
from innate symmetry, the resolution achieved with electron tomography
is lower, but still sufficient for evaluating the topology of
organelles or distributions of macromolecular assemblies across the
surface of a virus.
Click Here for more about
these applications and the cryo-EM facilities at the NYSBC.
Click Here to read a primer
about how to get started with your own cryoEM project.
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