A5027958286- Advanced Electron Microscopy Techniques and Applications
- Electron and X-Ray Spectroscopy Techniques
- Advanced X-ray Imaging Techniques
- RNA and protein synthesis mechanisms
- Enzyme Structure and Function
- Bacteriophages and microbial interactions
- Photosynthetic Processes and Mechanisms
- Monoclonal and Polyclonal Antibodies Research
- Force Microscopy Techniques and Applications
- Advanced Fluorescence Microscopy Techniques
- ATP Synthase and ATPases Research
- Lipid Membrane Structure and Behavior
- Genomics and Phylogenetic Studies
- RNA Interference and Gene Delivery
- Integrated Circuits and Semiconductor Failure Analysis
- Hemoglobinopathies and Related Disorders
- RNA modifications and cancer
- Molecular Biology Techniques and Applications
- Cell Image Analysis Techniques
- Glycosylation and Glycoproteins Research
- Advanced Materials Characterization Techniques
- Mitochondrial Function and Pathology
- Protein Structure and Dynamics
- Erythrocyte Function and Pathophysiology
- HIV Research and Treatment
New York Structural Biology Center
2016-2025
Chan Zuckerberg Initiative (United States)
2023-2025
Columbia University
2015-2024
Simons Foundation
2022
NanoImaging Services
2012-2021
ORCID
2020
Scripps Research Institute
2006-2015
Torrey Pines Institute For Molecular Studies
2006-2014
La Jolla Alcohol Research
2013
University of California, San Diego
1992-2013
The HIV-1 envelope glycoprotein (Env) trimer contains the receptor binding sites and membrane fusion machinery that introduce viral genome into host cell. As only target for broadly neutralizing antibodies (bnAbs), Env is a focus rational vaccine design. We present cryo-electron microscopy reconstruction structural model of cleaved, soluble (termed BG505 SOSIP.664 gp140) in complex with CD4 site (CD4bs) bnAb, PGV04, at 5.8 angstrom resolution. structure reveals spatial arrangement...
This Meeting Review describes the proceedings and conclusions from inaugural meeting of Electron Microscopy Validation Task Force organized by Unified Data Resource for 3DEM (http://www.emdatabank.org) held at Rutgers University in New Brunswick, NJ on September 28 29, 2010. At workshop, a group scientists involved collecting electron microscopy data, using data to determine three-dimensional (3DEM) density maps, building molecular models into maps explored how assess models, other that are...
Single particle cryo-electron microscopy (cryoEM) is often performed under the assumption that particles are not adsorbed to air-water interfaces and in thin, vitreous ice. In this study, we fiducial-less tomography on over 50 different cryoEM grid/sample preparations determine distribution within ice overall geometry of grid holes. Surprisingly, by studying holes 3D from 1000 tomograms, have determined vast majority (approximately 90%) an interface. The implications observation...
Influenza Revealed virus, a single-stranded RNA is responsible for substantial morbidity and mortality worldwide. The influenza ribonucleoprotein (RNP) complex, which carries out viral replication transcription, central to the virus life-cycle host adaptation (see Perspective by Tao Zheng ). Structural characterization of RNP has been challenging, but Moeller et al. (p. 1631 , published online 22 November) Arranz 1634 now report structure assembly this using cryo-electron microscopy...
Cryo-FIB/SEM combined with cryo-ET has emerged from within the field of cryo-EM as method for obtaining highest resolution structural information complex biological samples in-situ in native and non-native environments. However, challenges remain conventional cryo-FIB/SEM workflows, including milling thick specimens vitrification issues, preferred orientation, low-throughput when small and/or low concentration specimens, that distribute poorly across grid squares. Here we present a general...
Mitochondria-ER membrane contact sites (MERCS) represent a fundamental ultrastructural feature underlying unique biochemistry and physiology in eukaryotic cells. The ER protein PDZD8 is required for the formation of MERCS many cell types, however, its tethering partner on outer mitochondrial (OMM) currently unknown. Here we identify OMM FKBP8 as using combination unbiased proximity proteomics, CRISPR-Cas9 endogenous tagging, Cryo-electron tomography, correlative light-electron microscopy....