Author

F. X. Ruiz

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· 3 Biochemistry· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Research Focus:protein structure prediction· 2 Organism:virus· 2 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

E. Arnold· 5 shared J. D. Bauman· 3 shared J. J. E. K. Harrison· 3 shared J. J. DeStefano· 2 shared J. Timm· 2 shared P. R. Griffin· 2 shared R. Yadav· 2 shared A. Chopra· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 26 mutual co-author links

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5 shared papersBiophysics

E. Arnold

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Author profile →

5 papers

Recent·Most cited

The Halo Library, a Tool for Rapid Identification of Ligand Binding Sites on Proteins Using Crystallographic Fragment Screening

A. Chopra, J. D. Bauman, F. X. Ruiz, E. Arnold

The paper introduces the Halo Library, a set of halogenated fragments that improves the success rate of X-ray crystallographic fragment screening by identifying binding sites and hot spots on proteins.

bioRxiv · Oct 17, 2022Biochemistry

Biochemical and structural insights into SARS-CoV-2 polyprotein processing by Mpro

R. Yadav, V. V. Courouble, S. K. Dey, J. J. E. K. Harrison, J. Timm, J. B. Hopkins, R. L. Slack, S. G. Sarafianos, F. X. Ruiz, P. R. Griffin, E. Arnold

The paper elucidates the structural basis and cleavage order of SARS-CoV-2 nsp7-11 polyprotein processing by Mpro, with implications for Mpro inhibition.

bioRxiv · May 27, 2022Biochemistry

Cryo-EM Structure of the Pol Polyprotein Provides Insights into HIV Maturation

J. J. E. K. Harrison, D. O. Passos, J. F. Bruhn, J. D. Bauman, L. Tuberty, J. J. DeStefano, F. X. Ruiz, D. Lyumkis, E. Arnold

The paper determines the cryo-EM structure of the HIV-1 Pol polyprotein intermediate, revealing how RT dimerization activates proteolytic processing by bringing PR monomers together.

bioRxiv · Oct 3, 2021 · PreprintBiophysics

Resolving the Dynamic Motions of SARS-CoV-2 nsp7 and nsp8 Proteins Using Structural Proteomics

V. Courouble, S. Dey, R. Yadav, J. Timm, J. Harrison, F. X. Ruiz, E. Arnold, P. R. Griffin

This study uses HDX-MS and XL-MS to analyze the structural dynamics of the full-length SARS-CoV-2 nsp7:nsp8 complex, revealing conformational flexibility and a different assembly model compared to SARS-CoV.

bioRxiv · Mar 6, 2021 · PreprintBiophysics

Crystal Structure of a Retroviral Polyprotein:Prototype Foamy Virus Protease-Reverse Transcriptase (PR-RT)

J. J. E. K. Harrison, S. Tuske, K. Das, F. X. Ruiz, J. D. Bauman, P. Boyer, J. J. DeStefano, S. H. Hughes, E. Arnold

This paper reports the crystal structure of prototype foamy virus protease-reverse transcriptase (PR-RT), revealing its monomeric architecture and domain organization compared to HIV-1 enzymes.

bioRxiv · Nov 23, 2020Biophysics