Simon Hall is Indiana University's newest flagship research building. The completion of construction and occupancy occurred in the fall of 2007. This building has an interdisciplinary science theme - housing faculty from many different scientific disciplines that have overlapping interests. Designed to encourage interdisciplinary study in structural biology, biochemistry, bioanalytical chemistry, bioorganic chemistry, biophysics, nanobiology/nanofabrication, biocomplexity, microbial biochemistry, and molecular virology, the facility redefines boundaries and broadens scientific advancement. In addition to over 220 researchers, the building houses several instrumentation facilities such as the DNA sequencing facility, NMR facility, Nanofabrication facility, Cryo-electron microscopy facility, and Physical Biochemistry Instrumentation Facility.
Building Manager: John Morrow (Send Email)
Location: SI 005C
Department Chair, Dr. Carl Bauer was recently featured in a recent IU Update.
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The MCF provides all the equipment necessary to facilitate research in all aspects of structural biology at IUB. The new Crystallization Automation Facility (CAF) allows high throughput protein crystallography by the use of advanced robotics. The home source Rigaku RU-H2R R-Axis IV X-Ray generator permits diffraction and data collection. Lastly, computational resources facilitate structure determination and refinement with the latest programs available. The facility encourages research endeavors in structural biology and provides a central resource for IUB users as well as surrounding Academic Institutions.
Contacts: Charles Dann III (Send Email), Ardian Soca Wibowo (Send Email)
Location: SI 401, SI 401A
A recently purchased state-of-the-art JEOL JEM 3200FS transmission electron microscope (TEM) is shared between the departments of Biochemistry, Chemistry and Biology. This instrument is designed for low dose, low temperature imaging and tomography of biological materials. The electron microscope is also equipped with an energy filter for zero-energy-loss imaging (for biological samples), elemental imaging and electron energy loss spectroscopy (EELS), a high angle annular dark field scanning TEM (HAADF-STEM) detector for Z-contrast imaging and an energy dispersive X-ray (EDX) spectrometer. Though these add-ons are mainly used for materials science applications, recent work has begun to explore the use of such materials science instrumentation with biological materials and the electron microscope here at IU is ideally suited for such explorations. The facility is also equipped with an FEI Vitrobot for robotic vitrification of isolated macromolecular assemblies. The manager of the TEM will assist with initial feasibility studies and project design, data processing and analysis and training users of the instrument.
Location: SI 032
The Indiana MetaCyt Initiative , as part of the MetaCyt Biochemical Analysis Center has underwritten the acquisition of an 800 MHz Varian Inova NMR spectrometer with a cryogenic probe system. This instrument will be placed along side an existing 600 MHz Varian Inova NMR spectrometer with a cryogenic probe. These two instruments will be located on the ground floor of Simon Hall and will comprise the MetaCyt Biomolecular NMR Laboratory, a state-of-the-art facility for biomolecular structure and dynamics determination. The Chemistry Department Nuclear Magnetic Resonance facility consists of seven Varian spectrometers in three laboratories with an experienced staff of professional Ph.D. scientists. The undergraduate teaching laboratory contains a full featured 200 MHz instrument. The Chemistry Department NMR lab features four Varian spectrometers from 300MHz to 500MHz for work on liquid samples. The 400 MHz spectrometers feature 4-nucleus probes and gradients for multidimensional and multinuclear NMR experiments. The 500 MHz instrument is a full featured 3 channel instrument with a variety of probes and 3 axis gradients. It is used to perform almost any modern NMR experiment from demanding BioNMR experiments to diffusion studies and microimaging.
Contact: David Giedroc (Send Email)
Location: SI 037
The Physical Biochemistry Instrumentation Facility supports research in structures, stabilities, and interactions of biomolecules. Thorough hands-on training, state-of-the-art instrumentation, and analysis software are available 24 hours a day, and equipment time may be booked a round the clock via a web-based reservation system. The PBIF is directed by a Ph.D. scientist who assists researchers in the design, implementation, and analysis of experiments and results.
The PBIF features optical instruments for the study of structure, folding, binding thermodynamics and kinetics, and quantitation experiments: a Perkin Elmer LS50B Luminescence Spectrometer; a Jasco J-715 Circular Dichroism Spectrometer with Peltier sample temperature control; an Amersham Biosciences Typhoon 9210 Variable Mode Imager equipped with the versatile ImageQuant TL analysis package; and a Varian Cary 100 Bio UV / Visible Spectrometer for oligonucleotide melting studies. Other available instrumentation includes: a Microcal Isothermal Titration Calorimeter (VP- ITC); a Beckman Coulter Optima XL-I Analytical Ultracentrifuge with both absorbance and interference capabilities for probing size and associative properties; a Packard 1600TR Scintillation Counter for quantitation of assays and substrates; and a BIA CORE 3000 Surface Plasmon Resonance instrument that is capable of detailed, direct binding measurements and kinetic analysis of nucleotides and proteins. A recently purchased Malvern Zetasizer Nano-S dynamic light scattering instrument for quick molecular size characterizations has also been added to the PBIF capabilities.
Contact: Soca Wibowo (Send Email)
Location: SI 033
The Laboratory for Biological Mass Spectrometry is located in Simon Hall 115 as well as Chemistry 235. It houses equipment for mass spectrometric characterization of proteins, lipids, carbohydrates and metabolites. Major instrumentation include a Synapt G2 HDMS, an LTQ Orbitrap, an LTQ Velos Pro and a QTRAP 4000. The Laboratory performs a variety of analyses. It specializes in the identification and characterization of protein-interactions, protein post-translational modifications, and quantitative comparisons of complex samples.
Contacts: Jon Trinidad (Send Email)
Location: SI 115