The Rubinstein Laboratory

 

​Coupland, Karimi, Bueler, Liang, Courbon, Di Trani, Wong, Saghian, Youn, Wang, and Rubinstein (2024). High-resolution cryo-EM of V-ATPase in native synaptic vesicles. Science 385, 168-74.

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Courbon, Palme, Mann, Richter, Imming, and Rubinstein, J.L. (2023). Mechanism of mycobacterial ATP synthase inhibition by squaramides and second generation diarylquinolines. EMBO Journal e113687.

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Wang, Bueler, and Rubinstein (2023). Structural basis of V-ATPase VO region assembly by Vma12p, 21p, and 22p. PNAS 120, e2217181120.

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Liang, Plourde, Bueler, Liu, Brzezinski, Vahidi, Rubinstein (2023). Structure of mycobacterial respiratory Complex I. PNAS e2214949120.

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Di Trani, Moe, Riepl, Saura, Kaila, Brzezinski, Rubinstein (2022). Structural basis of mammalian Complex IV inhibition by steroids. PNAS 119, e2205228119

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Guo and Rubinstein (2022). Structure of ATP synthase under strain during catalysis. Nature Communications 13, 2232.

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Keon, Benlekbir, and Rubinstein (2022). Cryo-EM of the yeast VO complex reveals distinct binding sites for macrolide V-ATPase inhibitors. ACS Chemical Biology 17, 619-28.

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Vasanthakumar, Keon, Bueler, Jaskolka, and Rubinstein, (2022). Coordinated conformational changes in the V1 complex during V-ATPase reversible dissociation. Nature Structural and Molecular Biology 29, 430-9.

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Yanofsky, Di Trani, Kroll, Abdelaziz, Imming, Brzezinski, and Rubinstein (2021). Structure of mycobacterial CIII2CIV2 respiratory supercomplex bound to the tuberculosis drug candidate telacebec (Q203). eLife 10:e71959

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Guo H, Courbon GM, Bueler SA, Mai J, Liu J, Rubinstein JL (2021). Structure of mycobacterial ATP synthase bound to the tuberculosis drug bedaquiline. Nature 589, 143-147

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Tan YZ, Rubinstein JL (2020). Through-grid wicking enables high-speed cryoEM specimen preparation. Acta Crystallogr D76, 1092-1103.

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Guo H, Franken E, Deng Y, Benlekbir S, Singla Lezcano G, Janssen B, Yu L, Ripstein ZA, Tan YZ, Rubinstein JL (2020) Electron-event representation data enable efficient cryoEM file storage with full preservation of spatial and temporal resolution. IUCrJ 7, 860-869.
 

Abbas YM, Wu D, Bueler SA, Robinson CV, Rubinstein JL (2020). Structure of V-ATPase from the mammalian brain. Science 367, 1240-1246.
 

Ripstein ZA, Vahidi S, Houry WA, Rubinstein JL, Kay LE (2020). A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery. eLife e52158.

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Rubinstein JL, Guo H, Ripstein ZA, Haydaroglu A, Au A, Yip CM, Di Trani JM, Benlekbir S, Kwok T (2019). Shake-it-off: a simple ultrasonic cryo-EM specimen-preparation device. Acta Crystallogr D75, 1063-1070.

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Vasanthakumar T, Bueler SA, Wu D, Beilsten-Edmands V, Robinson CV, Rubinstein JL (2019). Structural comparison of the vacuolar and Golgi V-ATPases from Saccharomyces cerevisiae. Proc Natl Acad Sci (USA) 116, 7272-7277.

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Guo H, Suzuki T, and Rubinstein, JL. (2019). Structure of a bacterial ATP synthase. eLife 8:e43128.

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Wiseman B, Nitharwal R et al. (2018). Structure of a functional obligate complex III2IV2 respiratory supercomplex from Mycobacterium smegmatis. Nature Structural and Molecular Biology 25, 1128-1136.

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Sun C, Benlekbir S, Venkatakrishnan P, Wang Y, Hong S, Hosler J, Tajkhorshid E, Rubinstein JL, Gennis RB (2018). Structure of the alternative complex III in a supercomplex with cytochrome oxidase. Nature 557, 123-6.

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Guo H, Bueler SA, and Rubinstein JL (2017). Atomic model for the dimeric FO region of mitochondrial ATP synthase. Science 358, 936-40.

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Ripstein ZA, Huang R., Augustyniak R, Kay LE, and Rubinstein JL. (2017). Structure of a AAA+ unfoldase in the process of unfolding substrate. eLife 10.7554/eLife.25754

 

Punjani A, Rubinstein JL, Fleet DJ, Brubaker MA. (2017). Algorithmic innovation removes the computational bottleneck in cryo-EM. Nature Methods 14, 290-6.

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Mazhab-Jafari MT, Rohou A, Schmidt C, Bueler SA, Benlekbir S, Robinson CV, and Rubinstein JL. (2016). Atomic model for the membrane-embedded VO motor of a eukaryotic V-ATPase. Nature 539, 118-122.

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Wilson MD, Benlekbir S, Fradet-Turcotte A, Sherker A, Julien J-P, McEwan A, Noordermeer SM, Sicheri F, Rubinstein JL, and Durocher D. (2016). The structural basis of modified nucleosome recognition by 53BP1. Nature 536, 100-3.

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Huang R, Ripstein ZA, Augustyniak R, Kay LE, and Rubinstein JL. (2016). Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM solution NMR study. PNAS 113, E4190–E4199.

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Zhou A, Rohou A, Schep DG, Bason JV, Montgomery MG, Walker JE, Grigorieff N, Rubinstein JL. (2015). Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM. eLife e10180 [BioRxiv:11 Aug 2015]

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Rubinstein JL, and Brubaker MA. (2015). Alignment of cryo-EM movies of individual particles by optimization of image translations. Journal of Structural Biology 192, 188-95. [ArXiv:1409.6789]

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Zhao J, Benlekbir S, and Rubinstein JL. (2015). Cryo-EM observation of rotational states in a eukaryotic V-ATPase. Nature 521, 241-5.

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Marr CR, Benlekbir S, and Rubinstein JL. (2014). Fabrication of carbon films with ~500 nm holes for cryo-EM with a direct detector device. Journal of Structural Biology 185, 42-7.

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