Structural Biology Research Facilities

Cryo-Electron Microscopy

The cryo-EM facility is equipped with an FEI Tecnai F20 200kV, field-emission gun microscope specifically designed for high-resolution imaging of both stained and unstained cryogenically frozen samples. The instrument is suitable for imaging samples ranging from 200kDa protein complexes to entire prokaryotic cells. It is equipped with software for tomographic data collection. Images may are acquired on film or with a high-sensitivity, 4k x 4k-pixel Gatan CCD camera. The facility also has two Leica Ultracut microtomes for both ambient and cryogenic sectioning, a FEI Vitrobot sample preparation robot, and access to a Tecnai T12 electron microscope through the HRIF imaging core.



Beckman XL-A Analytical Ultracentrifuge

                The Analytical Ultracentrifuge is an ultracentrifuge equipped with an optical system that makes it possible to determine the distribution of macromolecules in the centrifuge cell during centrifugation. This instrument is used for either Sedimentation Velocity or Sedimentation Equilibrium experiments. These types of experiments are capable of providing information about macromolecular size, shape, and weight. For associating systems the data can be analyzed to obtain both the stoichiometry and the dissociation constant.

X-ray Crystallography

The X-ray crystallography facilities include high-throughput nano-crystallization systems for both aqueous and membrane proteins, three x-ray generators including a high-brilliance X-ray system with image plate detectors.  The equipment is complimented by a suite of software programs for structure determinations, modeling and in silico drug design.  In addition, as a member of the Southeast Regional Collaborative Access Team (SER-CAT) the university has dedicated access to two automated synchrotron X-ray beamlines at the Argonne National Synchrotron facility located in Chicago, Illinois.




Bruker Avanced 700 and 850 MHz Spectrometers

High-Field NMR spectroscopy is a highly versatile tool useful in a wide range of structural biology applications. It can be used to determine the three dimensional structures of biological macromolecules, e.g., proteins (including membrane proteins), nucleic acids, complex carbohydrates, as well as their various complexes (e.g., protein-RNA) directly in solution under physiologically meaningful conditions. 

In addition, it allows a study of protein dynamics (including detection of excited states). Equally important applications of NMR spectroscopy include drug discovery and design, and metabolic profiling of biofluids.



Mass Spectrometer Facility

Mass spectrometry can be used a variety of ways to explore protein structure. Incubating proteins with heavy water (D2O) selectively labels the amide protons with deuterium, a function of the exposure of individual residues to the solvent. Robotic technology (shown in the photo) is used to carry out complex kinetics. High-resolution mass spectrometry allows distinction between the increase in mass due to a naturally occurring 13C (1.003354) and incorporation of 2H (1.006277). The difference is 2.923 mDa.

The mass spectrometer is also used for crosslinking experiments designed to calculate inter-residue distances in proteins. A newer instrument combines high-resolution with extremely high-speed analysis, broadening applications of mass spectrometry into peptides and complex lipids.