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Brandeis Electron Microscopy Facility- The Louise Mashal Gabbay Cellular Visualization Center

Brandeis University

Contact Info:

Berith Isaac

415 South St

Waltham, MA 02453

https://www.brandeis.edu/science/resources/electron-microscope/index.html

Grants and Identifiers:

RRID: RRID:SCR_026272

Instrumentation:

Leica EM AFS2 Freeze Substitution Device

Leica EM AFS2 is a freeze substitution platform that performs freeze substitution and progressive lowering of temperature (PLT) techniques and allows low temperature embedding and polymerization of resins. The Leica EM FSP (freeze substitution processor), an automatic reagent handling system combined with the Leica EM AFS2, dispenses reagents for both freeze substitution and PLT applications. The LED illumination from within the chamber and the attached stereomicroscope for viewing and positioning of samples ensures ease of use. [Product Link]

RRID:SCR_020230

cite this instrument

EMS 975 Large Chamber Turbo Evaporator

The EMS 975 allows for carbon evaporation, metal evaporation from both baskets and crucibles and sputter coating option. A range of techniques can be practiced including carbon support films and replicas for TEM, carbon/metal evaporation, low angle shadowing

FEI TF20 TEM

TF20 sider loading cryo TEM

FEI Tundra Cryo-TEM

Cryo-TEM with semi autoloader

FEI Vitrobot Mark iv

Cryo fixation system for TEM

(Equipment No Longer Active At this Facility)

Leica AFS2 Automated Freeze Substitution Machine

Leica UC6 Ultramicrotome

Ultrathin sectioning and cryo sectioning for TEM

Philips Morgagni TEM

100Kv TEM

(Equipment No Longer Active At this Facility)

Thermo Fisher/FEI FEI Tundra Cryo-TEM

Cryo-TEM with Semi Autoloader

Tousimis Critical Point Dryer Samdri-PVT-3D

Services Provided:

Cryo-Electron Microscopy

Cryo-Electron Tomography

Immuno Electron Microscopy

Transmission Electron Microscopy

Relevant Publications:

1.) Henshaw RJ, Moon J, Stehnach MR, Bowen BP, Kosina SM, Northen TR, Guasto JS, Floge SA (2024 Dec). Metabolites from intact phage-infected Synechococcus chemotactically attract heterotrophic marine bacteria. Nature microbiology, 9(12), 3184-3195. doi: 10.1038/s41564-024-01843-2. ID: 39548345.


2.) Curtis Z, Escudeiro P, Mallon J, Leland O, Rados T, Dodge A, Andre K, Kwak J, Yun K, Isaac B, Martinez Pastor M, Schmid AK, Pohlschroder M, Alva V, Bisson A (2024 Oct). Halofilins as emerging bactofilin families of archaeal cell shape plasticity orchestrators. Proceedings of the National Academy of Sciences of the United States of America, 121(40), e2401583121. . ID: 39320913.


3.) Videbæk TE, Hayakawa D, Grason GM, Hagan MF, Fraden S, Rogers WB (2024 Jul 5). Economical routes to size-specific assembly of self-closing structures. Science advances, 10(27), eado5979. . ID: 38959303.


4.) Wise DL, Escobedo-Lozoya Y, Valakh V, Gao EY, Bhonsle A, Lei QL, Cheng X, Greene SB, Van Hooser SD, Nelson SB (2024 Jun). Prolonged Activity Deprivation Causes Pre- and Postsynaptic Compensatory Plasticity at Neocortical Excitatory Synapses. eNeuro, 11(6), . . ID: 38777611.


5.) Dresselhaus EC, Harris KP, Blanchette CR, Koles K, Del Signore SJ, Pescosolido MF, Ermanoska B, Rozencwaig M, Soslowsky RC, Parisi MJ, Stewart BA, Mosca TJ, Rodal AA (2024 May 5). ESCRT disruption provides evidence against transsynaptic signaling functions for extracellular vesicles. bioRxiv : the preprint server for biology, (), . . ID: 38746182.


6.) Wei WS, Trubiano A, Sigl C, Paquay S, Dietz H, Hagan MF, Fraden S (2024 Feb 13). Hierarchical assembly is more robust than egalitarian assembly in synthetic capsids. Proceedings of the National Academy of Sciences of the United States of America, 121(7), e2312775121. . ID: 38324570.


7.) Draganova EB, Wang H, Wu M, Liao S, Vu A, Gonzalez-Del Pino GL, Zhou ZH, Roller RJ, Heldwein EE (2024 Jan). The universal suppressor mutation restores membrane budding defects in the HSV-1 nuclear egress complex by stabilizing the oligomeric lattice. PLoS pathogens, 20(1), e1011936. . ID: 38227586.


8.) Vasquez S, Marquez MD, Brignole EJ, Vo A, Kong S, Park C, Perlstein DL, Drennan CL (2023 Dec 18). Structural and biochemical investigations of a HEAT-repeat protein involved in the cytosolic iron-sulfur cluster assembly pathway. Communications biology, 6(1), 1276. . ID: 38110506.


9.) Stehnach MR, Henshaw RJ, Floge SA, Guasto JS (2023 Jul 24). Multiplexed microfluidic screening of bacterial chemotaxis. eLife, 12(), . . ID: 37486823.


10.) Pitsawong W, Pádua RAP, Grant T, Hoemberger M, Otten R, Bradshaw N, Grigorieff N, Kern D (2023 Apr). From primordial clocks to circadian oscillators. Nature, 616(7955), 183-189. . ID: 36949197.


11.) Hayakawa D, Videbaek TE, Hall DM, Fang H, Sigl C, Feigl E, Dietz H, Fraden S, Hagan MF, Grason GM, Rogers WB (2022 Oct 25). Geometrically programmed self-limited assembly of tubules using DNA origami colloids. Proceedings of the National Academy of Sciences of the United States of America, 119(43), e2207902119. . ID: 36252043.


12.) Thorsen MK, Draganova EB, Heldwein EE (2022 Jul). The nuclear egress complex of Epstein-Barr virus buds membranes through an oligomerization-driven mechanism. PLoS pathogens, 18(7), e1010623. . ID: 35802751.


13.) Walsh RB, Dresselhaus EC, Becalska AN, Zunitch MJ, Blanchette CR, Scalera AL, Lemos T, Lee SM, Apiki J, Wang S, Isaac B, Yeh A, Koles K, Rodal AA (2021 Aug 2). Opposing functions for retromer and Rab11 in extracellular vesicle traffic at presynaptic terminals. The Journal of cell biology, 220(8), . . ID: 34019080.


14.) Herrmann T, Torres R, Salgado EN, Berciu C, Stoddard D, Nicastro D, Jenni S, Harrison SC (2021 Feb). Functional refolding of the penetration protein on a non-enveloped virus. Nature, 590(7847), 666-670. . ID: 33442061.


15.) Draganova EB, Zhang J, Zhou ZH, Heldwein EE (2020 Jun 24). Structural basis for capsid recruitment and coat formation during HSV-1 nuclear egress. eLife, 9(), . . ID: 32579107.


Description:

The Brandeis EM facility offers wide variety of preparation and visualization ranging from standard 2D EM methods to high resolution 3D cryo-EM. Instruments, training and assisted use are available for Brandeis faculty, staff, and lab members, as well as members of the broader scientific community, including other academic institutions and for-profit organizations.