Research Lab Bench

Biochemistry

Research Facilities

Learn more about the instruments used for research in the Biochemistry Department

BIAcore 3000 Instrument

The BIAcore 3000 instrument integrates surface plasmon resonance (SPR) technology with a microfluidics system to monitor molecular interactions in real time at concentrations ranging from pM to mM. This label-free technology can detect a wide range of molecular masses from 180Da to >1000kDa. The high sensitivity and high through-put capabilities allows for the detection of drug-protein, hormone-protein, protein-protein, DNA-protein, carbohydrate-protein, and lipid-protein interactions. The ability to interface with mass spectrometers provides discovery-based research in proteomic studies. For more information about SPR technology, theory, and applications, please see the BIAcore presentation (PDF).


The BIAcore 3000 instrument is housed in the Department of Biochemistry and is available to all Medical College of Wisconsin faculty and staff who have been trained and demonstrate the ability to use microfluidic-based instrumentation. Training and consultation are available on an appointment basis.

Fees

Note: A training period of no less than 4 hours is required before you can work unassisted on the instrument. BIAcore chips and special reagents are not included in the fee.

Training
Academic Users: $50/hour | Industrial/Non-Academic Users: $75/hour

Unassisted Use
Academic Users: $12.50/hour | Industrial/Non-Academic Users: $40/hour

Consultation (experimental design, data evaluation)
Academic Users: $50/hour | Industrial/Non-Academic Users: $75/hour

For more information contact:

Nancy Dahms, PhD
Medical College of Wisconsin
Department of Biochemistry
8701 Watertown Plank Rd.
Milwaukee, WI 53226
(414) 955-4698 | ndahms@mcw.edu

Biomolecular NMR at MCW

NMR Facility600 MHz NMR spectrometer. Cryoplatform is visible to the left of the magnet, RF console and workstation to the right.

The NMR Facility is an interdepartmental research service unit located in the Biochemistry Department. High-field NMR spectroscopy is a powerful technique for the study of biomolecular structure and dynamics. The facility provides service for routine 1D and 2D NMR methods, and can also provide consultation and collaborative assistance with the acquisition and analysis of multidimensional, multinuclear protein NMR spectra. The facility operates two Bruker 600 MHz and one 500 MHz NMR spectrometers, each equipped with 1H/13C/15N cryoprobes for enhanced sensitivity in biomolecular applications. In addition, a Bruker 300 MHz NMR spectrometer is available for routine analytical NMR of small molecules. For some long-term projects, the facility provides training for instrument operation and data analysis to investigators and research personnel. The facility operates on a fee-for-service basis and is open to faculty of the Medical College of Wisconsin and outside researchers.

The department houses state-of-the-art instrumentation dedicated to Structural Biology research. The facility includes chromatographic systems for protein purification, an in-house X-ray diffraction core and an automated crystallization system for high-throughput screening and optimization. High-end computer workstations have been set up for 3-D graphic visualization and crystallographic analysis.

The X-ray facility is located on the second floor of the Translational Biomedical Research Center (TBRC). The facility houses an X-ray diffraction system consisting of a Rigaku R-AXIS IV++ image plate detector system and MicroMax 007 generator equipped with Osmic confocal mirrors and an X-treme crystal cryocooler. The crystallization system includes a Hamilton STAR for solution making and a Phoenix equipped with a CrysCam for nanoliter crystallization and visualization. A fully automatic crystal incubator/imager (crystallization hotel) will soon be added to enhance throughput capacity.

The facility is open to faculty members of the Medical College of Wisconsin. Various levels of training are available and collaborative arrangements can be made to scientists both inside and outside of the MCW community.

Biochemistry Shared Research Instrumentation

The Biochemistry Department maintains several instruments for isolation and physical characterization of biomolecules and detection of their interactions. All are located on the second floor of the TBRC and include:

Jasco J-710 Circular dichroism spectropolarimeter
The Jasco J-710 circular dichroism (CD) spectropolarimeter is equipped with a thermally regulated sample compartment. Monitoring of the far-UV and/or near-UV CD spectra can provide valuable information about the secondary structure, thermal stability, or conformational state of a protein.
Contact: Nolan Kennedy, nolkennedy@mcw.edu

Photon Technologies Inc. QuantaMaster™ spectrofluorometer
The QuantaMaster™ spectrofluorometer is outfitted with dual excitation and emission monochromators for high sensitivity, a thermally regulated sample compartment, and Glan Thompson polarizers for fluorescence anisotropy measurements. The instrument is suitable for emission/excitation scanning experiments, fluorescence experiments requiring synchronous scanning of the excitation and emission monochromators, time based fluorescence measurements, fluorescence resonance energy transfer experiments and fluorescence anisotropy measurements.
Contact: Francis Peterson, fpeterso@mcw.edu | Davin Jensen, djensen@mcw.edu

MicroCal VP - Isothermal Titration Calorimetry
The MicroCal VP-ITC is capable of measuring heat evolution as little as 0.4 nanoJ/sec. This instrument is suitable for the studies of protein-ligand and protein-protein interactions and provides the biochemists with reliable measurements of binding constants in the range of 103-109 M-1 as well as the enthalpy and stoichiometry of interactions. ITC is a preferred technique to demonstrate the interaction between newly discovered binding partners in vitro.
Contact: Brian Smith, brismith@mcw.edu

Perseptive Biosystems Voyager DE-Pro MALDI mass spectrometer
The matrix-assisted laser desorption ionization (MALDI) mass spectrometer is used for routine mass determination of peptides, proteins and other macromolecules.
Contact: Davin Jensen, djensen@mcw.edu

Promega Maxwell-16 robot
This benchtop instrument provides fast automation of routine DNA, RNA or protein extractions resulting in reproducible yields and purity. Parallel multi-channel operation permit automated purification of milligram yields of up to 16 different recombinant proteins in less than one hour.
Contact: Davin Jensen, djensen@mcw.edu

Molecular Devices Flexstation 3 microplate reader
This benchtop instrument is a 5-mode microplate reader for use in a wide range of biochemical- and cell-based assays for basic research and drug discovery. This instrument is equipped with an 8-channel pipettor for 96-well-based assays based on absorbance, fluorescence intensity, fluorescence polarization, luminescence, and time-resolved fluorescence assays. It has high-efficiency tunable monochromator optics and a dedicated photomultiplier tube for luminescence assays.
Contact: Chad Koplinski, ckoplinski@mcw.edu | Francis Peterson, fpeterso@mcw.edu