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Principal Investigator: Yifan Cheng
Organization: UNIVERSITY OF CALIFORNIA, SAN FRANCISCO
Fiscal Year: 2020
Award: $292,301
Funding agency: National Institute of Allergy and Infectious Diseases
As a versatile structure determination technology, cryo-EM is an integrated part of the HARC Center. In the
past funding cycle, the Cryo-EM Core has engaged in technology development of single-particle cryo-EM, and
has made major contributions to the recent technological breakthroughs in single particle cryo-EM that has led
to a resolution revolution. Briefly, we developed one of the very first programs to correct beam-induced image
motion, developed a novel approach of using conformation-specific Fabs to facilitate single particle cryo-EM
studies, determined the first atomic structure of an integral membrane protein that changed the perspective of
the entire structural biology community, determined atomic structures of integral membrane proteins in lipid
nanodiscs and developed a novel saposin-based lipid nanoparticle system for single particle cryo-EM studies
of small integral membrane proteins. In this renewal, we will both focus on methodology development as well
as application of state-of-the-art single particle cryo-EM technology to solve critical HIV structural biology
questions.
Terms: <20S Catalytic Proteasome><20S Core Proteasome><20S Proteasome><20S Proteosome><3-D><3-Dimensional><3D><AIDS Virus><APF-1><ATP-Dependent Proteolysis Factor 1><Acquired Immune Deficiency Syndrome Virus><Acquired Immunodeficiency Syndrome Virus><Algorithms><Antigen Binding Fragment><Antiviral Agents><Antiviral Drugs><Antivirals><Biochemical><Biologic Models><Biological Models><CBF><CUL5><CUL5 gene><Cell Body><Cells><Collaborations><Communities><Complex><Core-Binding Factor><Cryo-electron Microscopy><Cryoelectron Microscopy><Crystallization><Development><Electron Cryomicroscopy><Environment><Enzyme Gene><Enzymes><Fab Fragments><Fab Immunoglobulins><Family><Funding><Goals><HIV><HIV Infections><HMG-20><HTLV-III Infections><HTLV-III-LAV Infections><High Mobility Protein 20><Human Immunodeficiency Viruses><Human T-Lymphotropic Virus Type III Infections><Image><Immunoglobulin, F(ab) Fragment><Integral Membrane Protein><Intrinsic Membrane Protein><Investigators><Ion Channel><Ionic Channels><LAV-HTLV-III><Laboratories><Lipids><Lymphadenopathy-Associated Virus><Macropain><Macroxyproteinase><Membrane><Membrane Channels><Membrane Protein Gene><Membrane Proteins><Membrane-Associated Proteins><Methodology><Methods><Model System><Molecular Configuration><Molecular Conformation><Molecular Stereochemistry><Motion><Multicatalytic Proteinase><Names><Negative Staining><Pathway interactions><Phage Display><Play><Procedures><Production><Prosome><Proteasome><Proteasome Endopeptidase Complex><Proteins><Proteosome><Publishing><Research Personnel><Researchers><Resolution><Role><Saposins><Spliceosomes><Structure><Surface Proteins><System><TRPV1><TRPV1 gene><Technology><Testibumin><Time><Transmembrane Protein><Transmembrane Protein Gene><Ubiquitin><VACM-1><VACM1><Virus-HIV><anti-viral agents><anti-viral drugs><anti-viral immunity><anti-virals><antiviral immunity><base><conformation><conformational state><cryo-EM><cryoEM><developmental><imaging><improved><lipid nanoparticle><member><membrane structure><molecular imaging><molecule imaging><multicatalytic endopeptidase complex><nano disk><nanodisc technology><nanodisk><new approaches><new technology><novel><novel approaches><novel strategies><novel strategy><novel technologies><particle><pathway><programs><protein complex><protein structure><protein structures><proteins structure><reconstruction><scale up><screening><social role><structural biology><success><tech development><technology development><three dimensional>