REPRESENTATIVE PUBLICATIONS
A complete list of publications can be found on Pubmed
Wang, Bueler, and Rubinstein (2023). Structural basis of V-ATPase VO region assembly by Vma12p, 21p, and 22p. PNAS 120, e2217181120.
Liang, Plourde, Bueler, Liu, Brzezinski, Vahidi, Rubinstein (2023). Structure of mycobacterial respiratory Complex I. PNAS e2214949120.
Di Trani, Moe, Riepl, Saura, Kaila, Brzezinski, Rubinstein (2022). Structural basis of mammalian Complex IV inhibition by steroids. PNAS 119, e2205228119
Guo and Rubinstein (2022). Structure of ATP synthase under strain during catalysis. Nature Communications 13, 2232.
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.
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.
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
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
Tan YZ, Rubinstein JL (2020). Through-grid wicking enables high-speed cryoEM specimen preparation. Acta Crystallogr D76, 1092-1103.
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.
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.
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.
Guo H, Suzuki T, and Rubinstein, JL. (2019). Structure of a bacterial ATP synthase. eLife 8:e43128.
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.
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.
Guo H, Bueler SA, and Rubinstein JL (2017). Atomic model for the dimeric FO region of mitochondrial ATP synthase. Science 358, 936-40.
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.
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.
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.
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.
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]
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]
Zhao J, Benlekbir S, and Rubinstein JL. (2015). Cryo-EM observation of rotational states in a eukaryotic V-ATPase. Nature 521, 241-5.
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.