A5014815684- Advanced Electron Microscopy Techniques and Applications
- Electron and X-Ray Spectroscopy Techniques
- Enzyme Structure and Function
- Advanced X-ray Imaging Techniques
- Metalloenzymes and iron-sulfur proteins
- RNA modifications and cancer
- Cellular transport and secretion
- Lipid Membrane Structure and Behavior
- Nanowire Synthesis and Applications
- Photovoltaic System Optimization Techniques
- solar cell performance optimization
- Pancreatitis Pathology and Treatment
- Thermal Regulation in Medicine
- International Science and Diplomacy
- Mass Spectrometry Techniques and Applications
- Parathyroid Disorders and Treatments
- Ion-surface interactions and analysis
- Bacterial Identification and Susceptibility Testing
- Radiation Dose and Imaging
- Advanced Materials Characterization Techniques
- Calcium signaling and nucleotide metabolism
- scientometrics and bibliometrics research
- Distributed and Parallel Computing Systems
- Genomics and Phylogenetic Studies
- Quantum and electron transport phenomena
New York Structural Biology Center
2020-2025
New York Genome Center
2024
Simons Foundation
2022
Single-particle cryo-electron microscopy (cryoEM) is a swiftly growing method for understanding protein structure. With increasing demand high-throughput, high-resolution cryoEM services comes greater rapid and automated grid sample screening. During screening, optimal grids conditions are identified subsequent data collection. Screening major bottleneck new projects because must be optimized several factors, including type, hole size, concentration, buffer conditions, ice thickness particle...
We report on the latest advancements in Microcrystal Electron Diffraction (3D ED/MicroED), as discussed during a symposium at National Center for CryoEM Access and Training housed New York Structural Biology Center. This snapshot describes cutting-edge developments various facets of field identifies potential avenues continued progress. Key sections discuss instrumentation access, research applications small molecules biomacromolecules, data collection hardware software, reduction finally...
Escherichia coli NADPH-dependent assimilatory sulfite reductase (SiR) reduces by six electrons to make sulfide for incorporation into sulfur-containing biomolecules. SiR has two subunits: an NADPH, FMN, and FAD-binding diflavin flavoprotein a siroheme/Fe4S4 cluster-containing hemoprotein. The molecular interactions that govern subunit binding have been unknown since the discovery of over 50 years ago because is flexible, thus intransigent traditional high-resolution structural analysis. We...
Cryo-electron microscopy (cryoEM) is a technology that facilitates structural sciences research by allowing wide range of molecular and cellular structures to be determined. With the expansion biomedical researchers utilizing cryoEM approaches there growing number instrumentation being installed in laboratories, departmental cores national facilities. Along with adoption these tools need lower barriers access workflows establish shared standard operating procedures. To help raise proficiency...
Adaptor protein complex-3 (AP-3) mediates cargo sorting from endosomes to lysosomes and lysosome-related organelles. Recently, it was shown that AP-3 adopts a constitutively open conformation compared the related AP-1 AP-2 coat complexes, which are inactive until undergoing large conformational changes upon membrane recruitment. How is regulated therefore an question. To understand mechanism of recruitment activation, we reconstituted human determined multiple structures in soluble...
Advancements in cryo-electron microscopy (cryoEM) techniques over the past decade have allowed structural biologists to routinely resolve macromolecular protein complexes near-atomic resolution. The general workflow of entire cryoEM pipeline involves iterating between sample preparation, grid and sample/grid screening before moving on high-resolution data collection. Iterating preparation is typically a major bottleneck for researchers, as every iterative experiment must optimize...
Journal Article The National Center for CryoEM Access and Training - Establishing a Cross-Facility-Honored Curriculum Get access Edward T Eng, Eng Training, Simons Electron Microscopy Center, New York Structural Biology York, NY, USA Corresponding author: eeng@nysbc.org Search other works by this author on: Oxford Academic Google Scholar Christina Zimanyi, Zimanyi Mahira Aragon, Aragon Eugene Y D Chua, Chua Elina Kopylov, Kopylov Charlie Dubbeldam, Dubbeldam Cathleen Castello, Castello...
Abstract Single particle cryo-electron microscopy (cryoEM) is a swiftly growing method for understanding protein structure. With increasing demand high-throughput, high-resolution cryoEM services comes greater rapid and automated grid sample screening. During screening, optimal grids conditions are identified subsequent data collection. Screening major bottleneck new projects because must be optimized over several factors, including type, hole size, concentration, buffer conditions, ice...
Abstract Summary CryoEM multi-grid screening is often a tedious process that demands hours of attention. Here, this protocol shows how to set up standard Leginon collection and Smart Autoscreen automate process. This can be applied the majority cryoEM holey foil grids. Advancements in cryo-electron microscopy (cryoEM) techniques over past decade have allowed structural biologists routinely resolve macromolecular protein complexes near-atomic resolution. The general workflow entire pipeline...
Adaptor protein complex 3 (AP-3) mediates cargo sorting from endosomes to lysosomes and lysosome-related organelles. Recently, it was shown that AP-3 is in a constitutively open, active conformation compared the related AP-1 AP-2 coat complexes, which are inactive until undergoing large conformational changes upon membrane recruitment. How regulated therefore an open question. To understand mechanism of recruitment activation, we reconstituted core human determined multiple structures...
Escherichia coli NADPH-dependent assimilatory sulfite reductase (SiR) reduces by six electrons to make sulfide for incorporation into sulfur-containing biomolecules. SiR has two subunits: an NADPH, FMN, and FAD-binding diflavin flavoprotein a siroheme/Fe4S4 cluster-containing hemoprotein. The molecular interactions that govern subunit binding have been unknown since the discovery of over 50 years ago because is flexible, thus intransigent traditional high-resolution structural analysis. We...
<title>Abstract</title> <italic>Escherichia coli</italic> NADPH-dependent assimilatory sulfite reductase (SiR) fixes sulfur for incorporation into sulfur-containing biomolecules. SiR is composed of two subunits: an NADPH, FMN, and FAD-binding diflavin iron siroheme/Fe<sub>4</sub>S<sub>4</sub> cluster-containing oxidase. How they interact has been unknown over 50 years because highly flexible, thus intransigent traditional X-ray or cryo-EM structural analysis. A combination the chameleon...
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Journal Article Microscope Operations at the National Center for CryoEM Access and Training (NCCAT) Get access Aygul Ishemgulova, Ishemgulova Training, Simons Electron Microscopy Center, New York Structural Biology York, NYUnited States Corresponding author: aishemgulova@nysbc.org Search other works by this author on: Oxford Academic Google Scholar Jing Wang, Wang Kasahun Neselu, Neselu Kashyap Maruthi, Maruthi Christina Zimanyi, Zimanyi Mahira Aragon, Aragon Elina Kopylov, Kopylov Joshua...
Advancements in cryo-electron microscopy (cryoEM) techniques over the past decade have allowed structural biologists to routinely resolve macromolecular protein complexes near-atomic resolution. The general workflow of entire cryoEM pipeline involves iterating between sample preparation, grid and sample/grid screening before moving on high-resolution data collection. Iterating preparation is typically a major bottleneck for researchers, as every iterative experiment must optimize...
Journal Article The National Center for CryoEM Access and Training: Broadening to Through Centralized Facilities Get access Edward T Eng, Eng Training, Simons Electron Microscopy Center, New York Structural Biology York, NY United States Corresponding author: eeng@nysbc.org Search other works by this author on: Oxford Academic Google Scholar Christina Zimanyi, Zimanyi Hui Wei, Wei Mahira Aragon, Aragon Eugene YD Chua, Chua Elina Kopylov, Kopylov Charlie Dubbeldam, Dubbeldam Cathleen...
Journal Article Evaluating the chameleon Sample Preparation Device: Case Studies Get access Mahira Aragon, Aragon Simons Electron Microscopy Center, New York Structural Biology York, NY, United StatesNational Center for CryoEM and Training, StatesSimons Resource Automated Molecular Microscopy, States Search other works by this author on: Oxford Academic Google Scholar Hui Wei, Wei Eugene YD Chua, Chua Joshua H Mendez, Mendez Bridget Carragher, Carragher Corresponding author: bcarr@nysbc.org...
Journal Article Improving Cryo-EM Ice Thicknesses Workflows on the Chameleon Sample Preparation Device Get access Eugene YD Chua, Chua Simons Electron Microscopy Center, New York Structural Biology York, NY, USA Search for other works by this author on: Oxford Academic Google Scholar Hui Wei, Wei USANational Resource Automated Molecular Microscopy, Mahira Aragon, Aragon Clinton S Potter, Potter Bridget Carragher Corresponding author; bcarr@nysbc.org and Microanalysis, Volume 28, Issue S1, 1...
An abstract is not available for this content so a preview has been provided. As you have access to content, full PDF via the ‘Save PDF’ action button.