Structural Biology and Biophysics facilities

About our research labs

Research in Structural Biology & Biophysics is world-class, as evidenced by the large number of punlidcations, and research grants awarded to Faculty members in this area. Some of the most important challenges facing mankind today, such as understanding Alzheimers Disease and the evolution of "superbugs" resistant to antibiotics, are being studied in our laboaboratories. The ltest hardware, the vast knowledge base of research group members, and the stimulation and challenging environment created for graduate students by the BMBB PhD Program, enables students to tackle whatever biological questions pose themselves during the formulation of their thesis.

Weekly Structyral Biology Club meeting provide a forum for students to present their research, listen and talk with visiting researchers and interact with other research lab members. Other opportunities for interaction come from more focused group meetings, such as those organized by the NMR users group and the Center for Metals in Biocatalysis.

Research facilities

Electron Paramagnetic Resonance

EPR is a powerful, versatile, nondestructive, and nonintrusive analytical method. EPR yields structural and dynamical information, even from ongoing chemical or physical processes without influencing the process itself. Conventional EPR is used to measure orientation and rotational motions in the time range from picoseconds to nanoseconds, while saturation transfer EPR extends this range to the microsecond time scale. Site-directed spin labeling (SDSL), in which Cys mutagenesis is used to place Cys-reactive spin labels at desired sites on a protein, is used to determine protein secondary and tertiary structure, and to measure structural changes that may be inaccessible to conventional structural techniques.

Optical Spectroscopy

Optical spectroscopy is a powerful, versatile, nondestructive, and nonintrusive analytical method.  BTC hosts instrumentation for time-resolved fluorescence (picoseconds to nanoseconds), phosphorescence (microseconds to milliseconds), and high-throughput screening (fluorescence lifetime and spectral platereaders). These instruments are used for identifying protein dynamics, interactions, and small-molecule effectors.

Muscle Mechanics

Single fibers from rabbit, rat, and scallop muscles are studied on this instrument to determine their mechanical properties. We are able to simultaneously measure maximal isometric force generation (how "strong" the muscle fibers are) and myosin ATPase activity (rate of "energy" used before and during a contraction), as illustrated in the figure at right. On other instruments we are also able to determine maximal shortening velocity (how "fast" fibers can contract) and maximal power output (how "powerful" fibers are) of single muscle fibers.

Nuclear Magnetic Resonance

Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool for studying protein structure and dynamics, and for characterizing molecular interactions. The NMR facility at the University of Minnesota ranks among the best in the world and the research of four different groups in the BMBB department is dedicated to using NMR spectroscopy to solve biological problems. Please visit our NMR web page and view our fine facility.

X-Ray Crystallography

The Kahlert Structrual Biology Laboratory (KSBL)

The biological molecules that make up our bodies have evolved exquisite ways to control and promote complex chemistries and communications that orchestrate our daily lives, as well as keep harmful disease causing “bugs” at bay. When these systems malfunction, or the immune system is overwhelmed, the effects can be catastrophic.

To understand the changes that lead to adverse effects to human health and also disease, we need to understand how the molecular “players” work. Most drugs and toxic compounds are small relative to the biological molecules they target. We therefore need to image the interactions on the scale of these smaller compounds. One of the major routes to obtaining highly detailed images of biological molecules at the level of the compounds to which they bind, is using a technique called X-ray crystallography. Results using this technique have impacted human health and disease in many ways. Improving drug efficacy and selectivity (reducing unwanted side-effects) through improved design; guiding vaccine development; understanding the evolution of multi-drug resistant organisms, and how to combat them; optimization of strategies for the removal of toxic compounds from the environment; engineering bacteria into factories for complex drug production.


Biophysical Technology Center
  • Director: J. Michael Autry, PhD
  • Spectroscopy Manager: Andrew R. Thompson, PhD
  • HTS Manager: Tory M. Schaaf, PhD
Center For Mass Spectrometry and Proteomics
  • Director: Dr. Timothy Griffin
  • Associate Director: Dr. Gary Nelsestuen
  • Manager: Pratik D. Jagtap
Kahlert Structural Biology Laboratory
  • Director: Dr. Carrie Wilmot
  • Manager: Dr. Ed Hoeffner
Nano Crystallization Facility
  • Director: Dr. Douglas Ohlendorf
  • Manager: Ke Shi
Nuclear Magnetic Resonance Facility
  • Director: Dr. Gianluigi Veglia
  • Structural Biology Manager: Dr. Youlin Xia
  • Metabolomics / Small Molecule Manager: Todd Rappe
  • Solid-state Manager: Dr. Gopinath Tata

Faculty research interests

X-Ray Crystallography
Nuclear Magnetic Resonance
Spectroscopy and other Biophysical Methods