Macromolecular Crystallography Facility (MCF)
Integrated with the Crystallization Automation Facility (CAF)
The MCF provides all the equipment necessary to facilitate research in all aspects of structural biology at Indiana University including a home source for X-Ray diffraction data collection from macromolecular crystals and computational support for structure determination and refinement. The home source includes two RAXIS IV + detectors and two X-Stream cryosystems. Researchers at IU are members of the Molecular Biology Consortium, which has a synchrotron beamline at the Advanced Light Source (ALS) in Berkeley. All IU macromolecular crystallographers and their students have access to the new 4.2.2 beamline for collection of high-resolution crystallographic data. Furthermore, the facility has recently been integrated with the Crystallization Automation Facility (CAF) comprised of three new instruments that provide high throughput robotic automated crystallization. The automation instruments found within the CAF include: (1) the Phoenix HT / RE, a drop setting robot that distributes user samples and potential crystallants in 96-3 format plates (up to 288 trials per plate). (2) The Alchemist is designed to generate customized crystallization screens based on initial crystallization "hits" to yield diffraction quality crystals. (3) The Minstrel HT/UV coupled with two Gallery 700 incubators allows for user-free storage and imaging of all crystallization trails. Image data are stored on a server that can be accessed remotely via the CrystalTrak Web software. The facility encourages research endeavors in structural biology and provides a central resource for IUB users.
For more information, please visit our website at: www.indiana.edu/~iumcf/
Location: SI 401, SI 401A
Transmission Electron Microscope (TEM) Facility
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
Nanoscale Characterization Facility (NCF)
The Nanoscale Characterization Facility (NCF) is housed on the ground floor in Simon Hall, our multidisciplinary sciences building, and has 2000 square ft of laboratory space and 1300 square ft of clean room space. The NCF will provide faculty, staff, postdoctoral fellows, and graduate and undergraduate students with state-of-the-art instrumentation for generating and characterizing materials having features with nanometer dimensions. We expect the NCF to grow over the next three to five years as a university resource, and the instrumentation within the facility will be available to all research groups at IU.
For fabrication, we have a UV exposure/alignment system (Optical Associates, Inc. 205S), stylus-based surface profiler (Veeco Dektak 6M), thin film deposition system (BOC Edwards Auto 306), spin coaters, high temperature furnace, and etch baths. In addition, we have a nanopattern generation system (Nabity NPGS) for electron beam (e-beam) lithography over small areas, coupled to our scanning electron microscope (Zeiss SMT 1430). Instruments for characterization include an environmental scanning electron microscope (FEI Quanta 600 FEG), a cryogenic transmission electron microscope (cryo-TEM, JEOL JEM-2200FS), and an atomic force microscope (Asylum Research MFP3D) coupled to a confocal fluorescence microscope (Nikon TE2000-U).
Location: SI 034
Nuclear Magnetic Resonance Laboratory
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.
Location: SI 037
Physical Biochemistry Instrumentation Facility (PBIF)
The Physical Biochemistry Instrumentation Facility supports research in structures, stabilities, and interactions of biomolecules. This state-of-the-art facility has been established to facilitate and encourage these research endeavors and to provide a centralized resource for training and education in modern physical biochemistry. 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/managed 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 Malvern Zetasizer Nano-S dynamic light scattering instrument for quick molecular size characterizations has also been added to the PBIF capabilities.
A recent addition to the PBIF is the Microscale Thermophoresis (MST) from Nanotemper. This platform is designed to quickly and easily quantitate interaction strength between biomolecules, be they proteins, small peptides, cofoactors, or ions. Other instruments include the Stopped Flow Spectrometer for quantitation of assays and substrates; the Multi-angle Ligth Scattering (MALS) Instrument and Refractive Index Dector to measure absolute molecular weight, size, and conformation of macromolecules in solution; a RT-PCR instrument for quantitation of gene expression as well as assay validation; and two Beckman Preparative Ultracentrifuge for pelleting protein and membrane samples to speeds of 100,000 rpm.
The doors to SI 033 (PBIF) are permanently locked. Users who need access to this facility must have clearance from the facility manager (SI 005A) and the MCB department office (SI 003). The fillable pdf form needed to initiate this request can be found here by clicking on the PBIF FORM link.
We hope researchers within the departments of IUB can benefit from the resources and capabilities held within the PBIF.
Contact: Giovanni Gonzalez-Gutierrez (firstname.lastname@example.org)
For more information, please visit our website at: www.indiana.edu/~physbio/
Location: SI 033
Laboratory for Biological Mass Spectrometry
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.
Location: SI 115, CH C233/C235