The actions of proteins and nucleic acids, and the way that they interact, is determined by their structure. The MOB faculty include many researchers with an interest in structural biology. They use a range of biophysical techniques to determine molecular structure, including X-ray crystallography, nuclear magnetic resonance, and cryogenic electron microscopy. Projects are wide ranging, and include virus-host interactions, the structural underpinning of bacterial sulfur metabolism, the structure of ribonucleoproteins, the mechanisms of membrane trafficking, muscle biophysics, and immunobiology.
Dr. Hank W. Bass's research focuses on the structural dynamics of chromosomes and chromatin. His lab employs 3D imaging, genetics, and cell biology techniques to investigate key processes such as meiosis, the telomere bouquet, and the nuclear envelope LINC complex. Ongoing projects include analyzing DNA replication timing in 3D, high-resolution profiling of chromatin structure to map transcription factor (TF) cistrome occupancy, and exploring the role of G-quadruplex (G4) DNA in gene regulation.
How certain viruses reach their replication centers in the nucleus to manipulate host genomes, and how host cells respond to this invasion is a fundamental question in virus-cell biology that the Francis lab aims to address. Using a multi-disciplinary approach involving single-virus live-cell imaging, structural biology, and genomics, his lab aims to understanding the underpinning principles of virus transport into the nucleus and its consequential effects, including structural, dynamic and contextual changes that encompass cellular adaptation.
Research in the Stagg lab is directed towards two tracks: the mechanisms of membrane trafficking, and high-throughput high-resolution cryo-EM. On the biological side, we determine the structure and mechanisms of medically relevant protein complexes involved in vesicle trafficking pathways. We have determined structures of COPII and clathrin coats as well as other membrane remodeling complexes. On the technical side, we develop experimental and computational methods to improve structure determination by cryo-EM.
The Stroupe Laboratory is interested in the structural underpinnings of bacterial sulfur metabolism. The superstar of this process is a multicomponent enzyme called sulfite reductase, which performs a unique six electron reduction of sulfite to sulfide for incorporation into sulfur-containing amino acids and cofactors. We use a combination of X-ray crystallography and cryogenic electron microscopy, along with biochemical assays, to understand this complex, but powerful, oxidoreductase.
The Taylor laboratory studies the molecular mechanism of muscle contraction using cryoEM. Current projects involve determining the structure of the thick, myosin-containing filaments from different types of striated muscle using filaments isolated from the muscle tissue itself. Future work will use Focused Ion Beam milling and cryo-lift-out of small pieces of muscle tissue frozen by different methods capable of millisecond time resolution to trap the various molecular steps of muscle contraction.
The Yin lab is interested in discovering the molecular mechanisms of individual proteins and protein assemblies in innate immunity, host-pathogen interactions, and membrane trafficking. Recent focus is on the endomembrane system, which is the focal point of both antimicrobial defense and cell homeostasis. Yin lab uses X-ray crystallography and cryo-EM, together with other biochemical and biophysical tools, to reveal the intricacies of complex biological processes.