MSNO March 2021 Membership meeting |
Date: March 31, 2021
Time: 7 pm - 8:10 pm
program
Cryogenic Electron Microscopy: From Fundamentals to Applications
Dr. Kungpeng Li, Cryo-Electron Microscopy Core Facility Manager
Case Western Reserve University, Cleveland, OH
Abstract. Cryogenic Electron Microscopy (Cryo-EM) is an approach that allows the observation of hydrated biological specimens in their native environment at cryogenic temperatures, allowing visualization of molecules down to the level of atomic details. This powerful analytical method has applications ranging across disciplines, including cancer, infectious diseases, neurodegenerative diseases, vision loss, drug addiction, and pain. This presentation will cover the fundamentals of this technique, and specific applications to viral and single particle samples.
Speaker Bio. Dr. Li has long-standing scientific interest in high-resolution cryo-EM technology and new sample preparation methods. His research over the last 15 years has focused on high-resolution cryo-EM reconstruction on virus and other single particle samples. As the CWRU Cryo-EM facility manager, he has extensive experience in all steps of cryo-EM technology, from cryo-EM grids preparation, modern advanced microscope operation, data analysis, and high-resolution 3D structure reconstruction.
Dr. Kungpeng Li, Cryo-Electron Microscopy Core Facility Manager
Case Western Reserve University, Cleveland, OH
Abstract. Cryogenic Electron Microscopy (Cryo-EM) is an approach that allows the observation of hydrated biological specimens in their native environment at cryogenic temperatures, allowing visualization of molecules down to the level of atomic details. This powerful analytical method has applications ranging across disciplines, including cancer, infectious diseases, neurodegenerative diseases, vision loss, drug addiction, and pain. This presentation will cover the fundamentals of this technique, and specific applications to viral and single particle samples.
Speaker Bio. Dr. Li has long-standing scientific interest in high-resolution cryo-EM technology and new sample preparation methods. His research over the last 15 years has focused on high-resolution cryo-EM reconstruction on virus and other single particle samples. As the CWRU Cryo-EM facility manager, he has extensive experience in all steps of cryo-EM technology, from cryo-EM grids preparation, modern advanced microscope operation, data analysis, and high-resolution 3D structure reconstruction.
Structural Studies of the AdeB Multidrug Efflux Pump
from Acinetobacter baumannii
Dr. Christopher Morgan, Postdoctoral Scholar
Department of Pharmacology , CWRU School of Medicine
Case Western Reserve University, Cleveland, OH
Abstract. The consistent rise in antibiotic resistance threatens to make standard bacterial infections difficult or even impossible to treat. Antibiotic evasion in multi-drug resistant (MDR) organisms is achieved through a number of mechanisms such as antibiotic modifying enzymes, ribosomal modifying enzymes and multidrug efflux pumps. Acinetobacter baumannii is a bacterial pathogen that displays a high level of multi-drug resistance. The A. baumanniiAdeB membrane protein is a major efflux transporter that mediates resistance to most clinically relevant antibiotics. Here, we elucidate the structure of AdeB in the presence of the substrate ethidium bromide using cryo-electron microscopy (cryo-EM). Using this technique, we have identified six distinct structures of AdeB that depict novel transient conformational states of the pump in action. This work characterizes an important antibiotic resistance mechanism and sheds light on a novel target for the development of new antibiotics.
Speaker Bio. Christopher E. Morgan graduated with a B.A. in Chemistry from Youngstown State University in 2013 and received his Ph.D. in Chemistry from Case Western Reserve University in 2018 working in the Tolbert Lab. Following graduation, he joined the Yu research group in 2018 as a postdoctoral scholar in the Department of Pharmacology at the CWRU School of Medicine. His current research focuses on utilizing Cryo-EM, computational and biophysical techniques to study the mechanisms of bacterial membrane transport proteins and their interactions with antibiotics, ribosome structure and function, and RNA structure
from Acinetobacter baumannii
Dr. Christopher Morgan, Postdoctoral Scholar
Department of Pharmacology , CWRU School of Medicine
Case Western Reserve University, Cleveland, OH
Abstract. The consistent rise in antibiotic resistance threatens to make standard bacterial infections difficult or even impossible to treat. Antibiotic evasion in multi-drug resistant (MDR) organisms is achieved through a number of mechanisms such as antibiotic modifying enzymes, ribosomal modifying enzymes and multidrug efflux pumps. Acinetobacter baumannii is a bacterial pathogen that displays a high level of multi-drug resistance. The A. baumanniiAdeB membrane protein is a major efflux transporter that mediates resistance to most clinically relevant antibiotics. Here, we elucidate the structure of AdeB in the presence of the substrate ethidium bromide using cryo-electron microscopy (cryo-EM). Using this technique, we have identified six distinct structures of AdeB that depict novel transient conformational states of the pump in action. This work characterizes an important antibiotic resistance mechanism and sheds light on a novel target for the development of new antibiotics.
Speaker Bio. Christopher E. Morgan graduated with a B.A. in Chemistry from Youngstown State University in 2013 and received his Ph.D. in Chemistry from Case Western Reserve University in 2018 working in the Tolbert Lab. Following graduation, he joined the Yu research group in 2018 as a postdoctoral scholar in the Department of Pharmacology at the CWRU School of Medicine. His current research focuses on utilizing Cryo-EM, computational and biophysical techniques to study the mechanisms of bacterial membrane transport proteins and their interactions with antibiotics, ribosome structure and function, and RNA structure
