The X-ray crystallography is a widely used technique for determining the atomic and molecular structure of biological macromolecules like proteins, nucleic acids, and their complexes.
Shared Facility
https://www.med.upenn.edu/jf/bsbcore/centers/crystallography.html
Researchers
The Marmorstein laboratory studies the molecular mechanisms of (1) epigenetic regulation (2) protein post- and co-translational modification with a particular focus on protein acetylation, and (3) enzyme signaling in cancer and metabolism. The laboratory uses a broad range of biochemical, biophysical and structural research tools (X-ray crystallography and cryo-EM) to determine macromolecular structure and mechanism of action. The laboratory also uses high-throughput small molecule screening and structure-based design strategies to develop protein-specific small-molecule probes to interrogate protein function and for preclinical studies.
Chemical Biology X-ray Crystallography cryoEM
We are interested in understanding on a structural and biochemical level how DNA and RNA molecules are maintained and processed by living cells. In addition to the mechanisms and regulation of genome replication and transcription, this includes processes such as DNA repair, site-specific and homologous recombination, transposition, condensation of chromosomes, chromosome pairing and segregation, and RNA trafficking and splicing. Our approach is to establish three-dimensional models of macromolecular assemblies relating to a particular biological question using X-ray diffraction methods and to then develop mechanistic and functional models that can be tested experimentally.
X-ray Crystallography cryoEM
The actin cytoskeleton plays an essential role in multiple cellular functions, including cytokinesis, vesicular trafficking, and the maintenance of cell shape and polarity. To accomplish these functions, the cytoskeleton undergoes constant remodeling into various forms of structural and functional networks, such as lamellipodia, filopodia, stress fibers and focal adhesions. Remodeling of the cytoskeleton of eukaryotic cells is a tightly regulated process, involving hundreds of actin-binding and signaling proteins. Additionally, many bacterial pathogens highjack the eukaryotic actin cytoskeleton during invasion. The main focus of the research in our lab is to understand the molecular basis for how protein-protein interaction networks bring together cytoskeleton scaffolding, nucleation, elongation, and signaling proteins to accomplish specific cellular functions. We are also interested in understanding the function of BAR domain-containing proteins, which are emerging as a critical linkage between signaling, the cytoskeleton and cellular membranes. Our lab is finally deeply invested in understanding the role of cytoskeleton dynamics in muscle cells, particularly the differentiated vascular smooth muscle cell. Our primary research tool is structural biology, including cryo-EM and X-ray crystallography. The atomic snapshots resulting from these structural methods provide a wealth of knowledge, but lack information about the function, dynamics and energetic aspects of protein-protein recognition. To obtain this kind of information we use a host of other approaches, including bio-informatics, biophysical and biochemical methods and collaborative cellular studies.
X-ray Crystallography cryoEM
Dr. Krishnaswamy studies molecular mechanisms underlying the reactions of blood coagulation. His laboratory investigates how the proteins of blood coagulation interact with each other and with membranes to yield a regulated clotting response to vascular injury or an unregulated response in thrombotic or bleeding disease.
X-ray Crystallography cryoEM
Kushol Gupta is a Research Assistant Professor in the Department of Biochemistry & Biophysics at the Perelman School of Medicine of The University of Pennsylvania, a member of the BMB graduate group, and directs the Johnson Foundation Structural Biology and Biophysics Core, a departmental resource that serves Penn and the greater region.
He is a structural biologist with expertise in both X-ray crystallography and solution biophysical methods, including small-angle X-ray and neutron scattering, light scattering, and analytical ultracentrifugation. His ongoing research focuses on retroviral integrases, their interaction with host factors, and a new class of drugs known as allosteric inhibitors of integrase (ALLINIs), which are potent antivirals against HIV. His research also includes other projects in the areas of phenylketonuria, RNA splicing, and site-specific recombination, highlighting the collaborative nature of research at Penn.
X-ray Crystallography X-ray Crystallography and Biophysics cryoEM
Our work focuses on the structural and chemical biology of metal-requiring enzymes in human disease as well as biosynthetic enzymes that generate complex terpenoid natural products. Our research incorporates modern techniques of structural biology, such as X-ray crystallography, small-angle X-ray scattering, and cryo-EM, as well as techniques rooted in bioinorganic, bioorganic, and biophysical chemistry.
Our group, along with the entire Penn Chemistry community, is committed to providing an open and engaging environment in which all persons are welcome and respected. We are a diverse group of faculty, staff, and students, and our strength derives from our diversity. We value the highest ideals of respect and dignity in our daily interactions as we maintain an environment that is free from all forms of discrimination, harassment, and intimidation. Whoever you are and wherever you are on your journey of scholarship in the molecular sciences, you are welcome here.
X-ray Crystallography cryoEM
The Liu Lab is affiliated with the Department of Biochemistry and Biophysics at the University of Pennsylvania Perelman School of Medicine. We utilized a battery of biochemical, cellular, and high-throughput sequencing approaches to study the function of RNA modifying enzymes and sex chromosome-encoded protein homologs in human physiology and disease.
X-ray Crystallography Mass Spectrometry