Skip to main content

Alberto Bartesaghi

Associate Professor of Computer Science
Computer Science
308 Research Drive, LSRC D338, Durham, NC 27708-0129

Overview


Dr. Bartesaghi is an Associate Professor in the departments of Computer Science, Biochemistry and Electrical and Computer Engineering at Duke University. The Bartesaghi Lab focuses on the development of machine learning approaches to determine the structure of macromolecular complexes of general biomedical interest using single-particle cryo-electron microscopy, cryo-electron tomography, and sub-volume averaging. Some of our targets include glycoproteins of enveloped viruses like HIV, Influenza and Ebola, transporters and channels involved in signaling and metabolism, GPCRs, DNA-targeting CRISPR-Cas surveillance complexes, and targets for cancer drugs. The lab also works more broadly in the fields of deep learning and artificial intelligence, computer vision, biomedical imaging, and high-performance computing.

Current Appointments & Affiliations


Associate Professor of Computer Science · 2022 - Present Computer Science, Trinity College of Arts & Sciences
Associate Professor of Biochemistry · 2018 - Present Biochemistry, Basic Science Departments
Associate Professor in the Department of Electrical and Computer Engineering · 2023 - Present Electrical and Computer Engineering, Pratt School of Engineering
Faculty Network Member of the Duke Institute for Brain Sciences · 2018 - Present Duke Institute for Brain Sciences, University Institutes and Centers

In the News


Published August 27, 2025
New Tool Cuts Protein Imaging Time from Months to Days
Published November 12, 2024
Uncovering Molecular Patterns Using AI
Published June 17, 2021
Chan Zuckerberg Initiative Invests in Duke Team’s Work to Improve Cryo-EM Images

View All News

Recent Publications


Strategies for studying discrete heterogeneity in situ using cryo-electron tomography.

Journal Article Current opinion in structural biology · December 2025 Structural variability plays a crucial role in enabling biological function, as the ability of proteins to adopt multiple conformations allows them to perform diverse cellular tasks. Cryo-electron tomography combined with subtomogram averaging and classifi ... Full text Cite

In situ structure determination of conformationally flexible targets using nextPYP.

Journal Article Nature protocols · August 2025 Single-particle cryoelectron tomography (SP-CET) is an imaging technique capable of determining the structure of proteins in their cellular environment at high-resolution. nextPYP is a web-based application designed to streamline the SP-CET structure deter ... Full text Cite

Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases.

Journal Article Sci Adv · November 2024 The intricate process of α-synuclein aggregation and fibrillization holds pivotal roles in Parkinson's disease (PD) and multiple system atrophy (MSA). While mouse α-synuclein can fibrillize in vitro, whether these fibrils commonly used in research to induc ... Full text Link to item Cite
View All Publications

Recent Grants


Structural and Functional Analysis of Nucleocytoplasmic Protein O-Glycosyltransferases in Plants

ResearchCollaborator · Awarded by National Institute of General Medical Sciences · 2023 - 2027

CC* Integration-Large: Scaling Scientific Workloads on Distributed Commodity GPUs and Storage through Campus-level RDMA Networking

ResearchSenior Investigator · Awarded by National Science Foundation · 2025 - 2027

Mechanisms of LRRK2 Mediated Neurotoxicity

ResearchCollaborating Investigator · Awarded by National Institute of Neurological Disorders and Stroke · 2018 - 2026

View All Grants

Education, Training & Certifications


University of Minnesota, Twin Cities · 2005 D.Phil.

External Links


Bartesaghi Lab