Tamir Gonen Explained

Fields:Membrane protein
Structural biology
cryoEM
MicroED
Workplaces:Howard Hughes Medical Institute
University of California, Los Angeles
Janelia Research Campus
University of Washington
Harvard Medical School
Alma Mater:University of Auckland (BS, PhD)
Thesis Title:Novel protein-protein interactions in the lens: a solution to the Mp20 enigma
Doctoral Advisor:Edward N. Baker
Joerg Kistler
Academic Advisors:Thomas Walz
Awards:
  • American Diabetes Association Career Development Award
  • Howard Hughes Medical Institute Early Career Scientist
  • A.L. Patterson Award of the American Crystallographic Association
Website:https://cryoem.ucla.edu/

Tamir Gonen (born 1975) is an American structural biochemist and membrane biophysicist best known for his contributions to structural biology of membrane proteins, membrane biochemistry and electron cryo-microscopy (cryoEM) particularly in electron crystallography of 2D crystals and for the development of 3D electron crystallography from microscopic crystals known as MicroED. Gonen is an Investigator of the Howard Hughes Medical Institute, a professor at the University of California, Los Angeles, the founding director of the MicroED Imaging Center at UCLA and a Member of the Royal Society of New Zealand.

Education

Gonen attended the University of Auckland in New Zealand and graduated with a Bachelor of Science double major in Inorganic Chemistry and Biological Sciences, followed by First Class Honors in Biological Sciences in 1998. He then obtained a Doctor of Philosophy in Biological Science in 2002 from the University of Auckland for research with by Edward N. Baker and Joerg Kistler.[1] Postdoctoral education was conducted at Harvard Medical School at the laboratory of Thomas Walz.

Research

Gonen's current research focuses on the structures and functions of medically important membrane proteins that are involved in homeostasis and method development in cryoEM, namely microcrystal electron diffraction (microED). He published the first atomic resolution structure determined by cryoEM detailing the structure of aquaporin-0 at 1.9Å resolution.[2]

Development of microcrystal electron diffraction

See main article: Microcrystal electron diffraction. The Gonen laboratory spearheaded the use of electron diffraction for the determination of protein structure from 3D nano crystals in a frozen hydrated state.[3] [4] [5] The method termed microED was established in 2013 with a proof of principle paper published in eLife.[6] In 2014 continuous rotation MicroED was established and demonstrated.[7] In 2015 the first novel structure was determined by MicroED for the protein alpha-synuclein at 1.4Å resolution[8] in collaboration with David Eisenberg and in 2016 microED yielded 1Å resolution data from protein nanocrystals where the phase could be solved ab initio.[9] MicroED has been used for drug discovery,[10] determination of membrane proteins such as ion channels[11] materials[12] and small organic molecules studied in a frozen hydrated state[13] [14] and extended to sub atomic resolution better than 0.8Å.[15]

Career

Honors

Memberships

2014 Royal Society of New Zealand

External links

Notes and References

  1. Gonen . Tamir . 2002 . Doctoral thesis . Novel protein-protein interactions in the lens: a solution to the Mp20 enigma . ResearchSpace@Auckland, University of Auckland . 2292/1094.
  2. Gonen. Tamir. Cheng. Yifan. Sliz. Piotr. Hiroaki. Yoko. Fujiyoshi. Yoshinori. Harrison. Stephen C.. Walz. Thomas. 2005-12-01. Lipid-protein interactions in double-layered two-dimensional AQP0 crystals. Nature. 438. 7068. 633–638. 10.1038/nature04321. 1476-4687. 1350984. 16319884. 2005Natur.438..633G.
  3. Doerr. Allison. 2014. Electron crystallography goes 3D with MicroED. Nature Methods. En. 11. 1. 6–7. 10.1038/nmeth.2797. 24524127. 38786632. 1548-7091.
  4. Web site: The Goldilocks Protocol: electrons sent in to put microcrystals to work for structural biology Stephen Curry. Curry. Stephen. 2013-11-19. the Guardian. en. 2018-07-31.
  5. Doerr. Allison. 2015. Structures from tiny crystals. Nature Methods. En. 12. 1. 37. 10.1038/nmeth.3238. 29710840. 1548-7091.
  6. Shi. Dan. Nannenga. Brent L.. Iadanza. Matthew G.. Gonen. Tamir. 2013-11-19. Three-dimensional electron crystallography of protein microcrystals. eLife. 2. e01345. 10.7554/eLife.01345. 2050-084X. 3831942. 24252878 . free .
  7. Nannenga. Brent L.. Shi. Dan. Leslie. Andrew G. W.. Gonen. Tamir. 2014. High-resolution structure determination by continuous-rotation data collection in MicroED. Nature Methods. 11. 9. 927–930. 10.1038/nmeth.3043. 1548-7105. 4149488. 25086503.
  8. Rodriguez. Jose A.. Ivanova. Magdalena I.. Sawaya. Michael R.. Cascio. Duilio. Reyes. Francis E.. Shi. Dan. Sangwan. Smriti. Guenther. Elizabeth L.. Johnson. Lisa M.. 2015-09-24. Structure of the toxic core of α-synuclein from invisible crystals. Nature. 525. 7570. 486–490. 10.1038/nature15368. 1476-4687. 4791177. 26352473. 2015Natur.525..486R.
  9. Sawaya. Michael R.. Rodriguez. Jose. Cascio. Duilio. Collazo. Michael J.. Shi. Dan. Reyes. Francis E.. Hattne. Johan. Gonen. Tamir. Eisenberg. David S.. 2016. Ab initio structure determination from prion nanocrystals at atomic resolution by MicroED. Proceedings of the National Academy of Sciences of the United States of America. 113. 40. 11232–11236. 10.1073/pnas.1606287113. 1091-6490. 5056061. 27647903. 2016PNAS..11311232S . free.
  10. Purdy. Michael D.. Shi. Dan. Chrustowicz. Jakub. Hattne. Johan. Gonen. Tamir. Yeager. Mark. 2017-12-30. MicroED Structures of HIV-1 Gag CTD-SP1 Reveal Binding Interactions with the Maturation Inhibitor Bevirimat. 10.1101/241182.
  11. Liu. Shian. Gonen. Tamir. 2018-05-03. MicroED structure of the NaK ion channel reveals a Na+ partition process into the selectivity filter. Communications Biology. En. 1. 1. 38. 10.1038/s42003-018-0040-8. 30167468. 6112790. 2399-3642.
  12. Vergara. Sandra. Lukes. Dylan A.. Martynowycz. Michael W.. Santiago. Ulises. Plascencia-Villa. Germán. Weiss. Simon C.. de la Cruz. M. Jason. Black. David M.. Alvarez. Marcos M.. 2017-11-16. MicroED Structure of Au146(p-MBA)57 at Subatomic Resolution Reveals a Twinned FCC Cluster. The Journal of Physical Chemistry Letters. 8. 22. 5523–5530. 10.1021/acs.jpclett.7b02621. 1948-7185. 5769702. 29072840. 1706.07902.
  13. Gallagher-Jones. Marcus. Glynn. Calina. Boyer. David R.. Martynowycz. Michael W.. Hernandez. Evelyn. Miao. Jennifer. Zee. Chih-Te. Novikova. Irina V.. Goldschmidt. Lukasz. 2018-01-15. Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp. Nature Structural & Molecular Biology. 25. 2. 131–134. 10.1038/s41594-017-0018-0. 29335561. 1545-9993. 6170007.
  14. The CryoEM Method MicroED as a Powerful Tool for Small Molecule Structure Determination. Jones. GC. Martynowycz. MW. 2018. en-US. 10.26434/chemrxiv.7215332. Hattne. J. Fulton. TJ. Stoltz. BM. Rodriguez. JA. Nelson. H. Gonen. T. ACS Central Science. 4. 11. 1587–1592. 30555912. 6276044.
  15. Hughes. Michael P.. Sawaya. Michael R.. Boyer. David R.. Goldschmidt. Lukasz. Rodriguez. Jose A.. Cascio. Duilio. Chong. Lisa. Gonen. Tamir. Eisenberg. David S.. 2018. Atomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks. Science. 359. 6376. 698–701. 10.1126/science.aan6398. 1095-9203. 29439243. 6192703. 2018Sci...359..698H.

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