Ed Brignole

Ed Brignole

Assistant Director, Cryo-EM Facility

Ed Brignole oversees the cryogenic electron microscopy facility and instructs users in all aspects of cryo-EM.





Ed Brignole received his PhD from Johns Hopkins University in Biochemistry, Cellular and Molecular Biology, investigating virus assembly with Wade Gibson. He went on to complete an NIH postdoctoral fellowship at the Scripps Research Institute with Francisco Asturias, before serving as an HHMI research scientist at MIT with Cathy Drennan. As the Assistant Director of the Cryogenic Electron Microscopy (Cryo-EM) Facility, Ed oversees the facility, located in MIT.nano. He instructs users in all aspects of cryo-EM — from experimental design and specimen preparation to imaging, processing, and 3D reconstruction. He also contributes to publications based on data gleaned from these studies. Once the facility is open, his day-to-day will involve acquisition and maintenance of the equipment, policy development and implementation, as well as image acquisition and evaluation of data quality. In 2017, Ed earned an MIT Infinite Kilometer Award for helping with the Department of Biology’s cryo-EM initiative. He is also a member of the American Association for the Advancement of Science.

Key Publications

  1. Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions. Cory, SA, Van Vranken, JG, Brignole, EJ, Patra, S, Winge, DR, Drennan, CL, Rutter, J, Barondeau, DP. 2017. Proc Natl Acad Sci U S A 114, E5325-E5334.
    doi: 10.1073/pnas.1702849114PMID:28634302
  2. The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism. Gibson, MI, Brignole, EJ, Pierce, E, Can, M, Ragsdale, SW, Drennan, CL. 2015. Biochemistry 54, 4112-20.
    doi: 10.1021/acs.biochem.5b00521PMID:26061898
  3. Generation of a stable, aminotyrosyl radical-induced α2β2 complex of Escherichia coli class Ia ribonucleotide reductase. Minnihan, EC, Ando, N, Brignole, EJ, Olshansky, L, Chittuluru, J, Asturias, FJ, Drennan, CL, Nocera, DG, Stubbe, J. 2013. Proc Natl Acad Sci U S A 110, 3835-40.
    doi: 10.1073/pnas.1220691110PMID:23431160
  4. The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years. Brignole, EJ, Ando, N, Zimanyi, CM, Drennan, CL. 2012. Biochem Soc Trans 40, 523-30.
    doi: 10.1042/BST20120081PMID:22616862
  5. Subunit architecture of general transcription factor TFIIH. Gibbons, BJ, Brignole, EJ, Azubel, M, Murakami, K, Voss, NR, Bushnell, DA, Asturias, FJ, Kornberg, RD. 2012. Proc Natl Acad Sci U S A 109, 1949-54.
    doi: 10.1073/pnas.1105266109PMID:22308316
  6. Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase. Ando, N, Brignole, EJ, Zimanyi, CM, Funk, MA, Yokoyama, K, Asturias, FJ, Stubbe, J, Drennan, CL. 2011. Proc Natl Acad Sci U S A 108, 21046-51.
    doi: 10.1073/pnas.1112715108PMID:22160671
  7. Single-particle electron microscopy of animal fatty acid synthase describing macromolecular rearrangements that enable catalysis. Brignole, EJ, Asturias, F. 2010. Methods Enzymol 483, 179-202.
    doi: 10.1016/S0076-6879(10)83009-5PMID:20888475
  8. A toolbox for ab initio 3-D reconstructions in single-particle electron microscopy. Voss, NR, Lyumkis, D, Cheng, A, Lau, PW, Mulder, A, Lander, GC, Brignole, EJ, Fellmann, D, Irving, C, Jacovetty, EL et al.. 2010. J Struct Biol 169, 389-98.
    doi: 10.1016/j.jsb.2009.12.005PMID:20018246
  9. Conformational flexibility of metazoan fatty acid synthase enables catalysis. Brignole, EJ, Smith, S, Asturias, FJ. 2009. Nat Struct Mol Biol 16, 190-7.
    doi: 10.1038/nsmb.1532PMID:19151726
  10. Enzymatic activities of human cytomegalovirus maturational protease assemblin and its precursor (pPR, pUL80a) are comparable: [corrected] maximal activity of pPR requires self-interaction through its scaffolding domain. Brignole, EJ, Gibson, W. 2007. J Virol 81, 4091-103.
    doi: 10.1128/JVI.02821-06PMID:17287260
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