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Cryoelectron microscopy structure of purified gamma-secretase at 12 A resolution

Publications associées (66)

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Microsecond Time-Resolved Cryo-Electron Microscopy

Oliver Florian Harder

Recently, single-particle cryo-electron microscopy emerged as a technique capable of determining protein structures at near-atomic resolution and resolving protein dynamics with a temporal resolution ranging from second to milliseconds. This thesis describ ...

EPFL2024

The synthesis of complex sugars is a key aspect of microbial biology. Cyclic beta-1,2-glucan (C beta G) is a circular polysaccharide critical for host interactions of many bacteria, including major pathogens of humans (Brucella) and plants (Agrobacterium). ...

Nature Portfolio2024

One-Dimensional "Ghost Imaging" in Electron Microscopy of Inelastically Scattered Electrons

Fabrizio Carbone, Giovanni Maria Vanacore, Ivan Madan, Ido Kaminer, Simone Gargiulo, Ebrahim Karimi

Entanglement and correlation are at the basis of quantummechanicsand have been used in optics to create a framework for "ghostimaging". We propose that a similar scheme can be used in anelectron microscope to exploit the correlation of electrons with theco ...

AMER CHEMICAL SOC2023

New Methods for the Integrative Dynamic Modeling of Biomolecular Structures

Sylvain Träger

The true understanding of most cellular functions is only really achievable through the structural determination of their underlying macromolecular assemblies. However, their size, large number of individual components and metastable states make their eluc ...

EPFL2021

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Proteins typically undergo dynamics on the microsecond to millisecond timescale, which is much faster than the time resolution of cryo-electron microscopy. Here, we propose a novel approach for microsecond time-resolved cryo-electron microscopy that involv ...

2021

Gold nanoparticles as a new tool in amyloid studies

Urszula Beata Cendrowska

The misfolding and self-assembly of proteins into fibrils is a hallmark of several neurodegenerative and systemic diseases. These disease-associated proteins have the propensity to form fibrils with a cross-Î² sheet structure, called amyloids. Amyloids can ...

EPFL2020

3D Poses Recovery in Single-Particle Cryo-EM from Learned Pairwise Projection Distances

Jelena Banjac

Single-particle cryo-electron microscopy (cryo-EM) is a technology that allows the observation and the high-resolution 3D structure determination of biomolecules. In this project, the goal is to estimate the angles at which we imaged the 2D projections fro ...

2020

Joint Angular Refinement and Reconstruction for Single-Particle Cryo-EM

Michaël Unser, Laurène Donati, Emmanuel Emilien Louis Soubies, Mona Zehni

Single-particle cryo-electron microscopy (cryo-EM) reconstructs the three-dimensional (3D) structure of bio-molecules from a large set of 2D projection images with random and unknown orientations. A crucial step in the single-particle cryo-EM pipeline is 3 ...

2020

High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica

Henning Paul-Julius Stahlberg, Jasenko Zivanov

Urease converts urea into ammonia and carbon dioxide and makes urea available as a nitrogen source for all forms of life except animals. In human bacterial pathogens, ureases also aid in the invasion of acidic environments such as the stomach by raising th ...

2020

Microfluidic protein isolation and sample preparation for high-resolution cryo-EM

Henning Paul-Julius Stahlberg, Inayathulla Mohammed

High-resolution structural information is essential to understand protein function. Protein-structure determination needs a considerable amount of protein, which can be challenging to produce, often involving harsh and lengthy procedures. In contrast, the ...

Proceedings of the National Academy of Sciences2019