Author

Z. A. Ripstein

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 5 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Assay:cryo-EM· 4 Organism:bacteria (other)· 2 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

J. L. Rubinstein· 5 shared L. E. Kay· 4 shared H. Guo· 2 shared J. M. Di Trani· 2 shared S. Benlekbir· 2 shared S. Vahidi· 2 shared A. Au· 1 shared A. Haydaroglu· 1 shared

Activity by Year

2017-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 26 mutual co-author links

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5 shared papersBiophysics

J. L. Rubinstein

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Author profile →

6 papers

Recent·Most cited

Flexible client-dependent cages in the assembly landscape of the periplasmic protease-chaperone DegP

R. W. Harkness, Z. A. Ripstein, J. M. Di Trani, L. E. Kay

The paper investigates how DegP forms flexible cage structures in response to different client sizes, revealing their structural diversity and functional roles in protein homeostasis.

bioRxiv · Oct 17, 2022Biophysics

Electron Event Representation (EER) data enables efficient cryoEM file storage with full preservation of spatial and temporal resolution

H. Guo, E. Franken, Y. Deng, S. Benlekbir, G. Singla Lezcano, B. Janssen, L. Yu, Z. A. Ripstein, Y. Z. Tan, J. L. Rubinstein

The paper introduces EER data format for cryoEM DDD movies, preserving spatial and temporal resolution without increasing file size.

bioRxiv · Apr 28, 2020Biophysics

An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR

S. Vahidi, Z. A. Ripstein, J. B. Juravsky, E. Rennella, A. L. Goldberg, A. K. Mittermaier, J. L. Rubinstein, L. E. Kay

This paper identifies an allosteric switch in Mycobacterium tuberculosis ClpP1P2 protease that regulates its activity through conformational changes, revealed by cryo-EM and methyl-TROSY NMR.

Proceedings of the National Academy of Sciences · Mar 2, 2020Peer-reviewedBiophysics

A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery

Z. A. Ripstein, S. Vahidi, W. A. Houry, J. L. Rubinstein, L. E. Kay

This study presents cryo-EM structures of the ClpXP complex from Neisseria meningitidis, revealing how ATP hydrolysis couples substrate unfolding and proteolysis.

bioRxiv · Dec 8, 2019Biophysics

Shake-it-off: A simple ultrasonic cryo-EM specimen preparation device

J. L. Rubinstein, H. Guo, Z. A. Ripstein, A. Haydaroglu, A. Au, C. M. Yip, J. M. Di Trani, S. Benlekbir, T. Kwok

The paper introduces a simple ultrasonic cryo-EM specimen preparation device that improves sample transfer efficiency and reduces air-water interface interactions.

bioRxiv · May 9, 2019Biophysics

Structure of a AAA+ unfoldase in the process of unfolding substrate

Z. A. Ripstein, R. Huang, R. Augustyniak, L. E. Kay, J. L. Rubinstein

The paper captures the structure of VAT, an AAA+ unfoldase, during substrate unfolding using cryo-EM, revealing a hand-over-hand mechanism.

bioRxiv · Feb 4, 2017Biochemistry