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*Indicates equal contribution by authors


  1. A.M. Levine, G. Bu, S. Biswas, E.H.R. Tsai*, A.B. Braunschweig* and B.L. Nannenga*. 2020. Crystal Structure and Orientation of Organic Semiconductor Thin Films by Microcrystal Electron Diffraction and Grazing-Incidence Wide-angle X-ray Scattering. Chemical Communications. 56:4204-4207 

  2. B.L. Nannenga*. 2020. MicroED methodology and development. Structural Dynamics. 7:014304 


  1. B.L. Nannenga*, and T. Gonen*. 2019. Microcrystal electron diffraction methodology and applications. MRS Bulletin. 44:956-960 

  2. F. Zhu, B.L. Nannenga, and M.A. Hayes*. 2019. Electrophoretic exclusion microscale sample preparation for cryo-EM structural determination of proteins. Biomicrofluidics. 13:054112 

  3. A. Thaker, K. Pushpavanam, T. Bista, S. Sapareto, K. Rege, B.L. Nannenga*. 2019. Protein‐facilitated gold nanoparticle formation as indicators of ionizing radiation. Biotechnology and Bioengineering. 116:3160-3167 

  4. N.A. Zatsepin, C. Li, P. Colasurd and B.L. Nannenga*. 2019. The complementarity of serial femtosecond crystallography and MicroED for structure determination from microcrystals. Current Opinions in Structural Biology. 58:286-293 

  5. B.L. Nannenga* and T. Gonen*. 2019. The cryo-EM method microcrystal electron diffraction (MicroED). Nature Methods. 16:369-379 


  1. B.L. Nannenga and T. Gonen*. 2018. MicroED: a versatile cryoEM method for structure determination. Emerging Topics in Life Sciences. 2:1-8 

  2. B.L. Nannenga, G. Bu and D. Shi*. 2018. The evolution and advantages of MicroED. Frontiers in Molecular Biosciences. 5:114 


  1. P. Krotee, J.A. Rodriguez, M.R. Sawaya, D. Cascio, F.E. Reyes, D. Shi, J. Hattne, B.L. Nannenga, M.E. Oskarsson, S. Philipp, S. Griner, L. Jiang, C.G. Glabe, G.T. Westermark, T. Gonen and D.S. Eisenberg*. 2017. Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity. eLife. 6:e19273 


  1. Nannenga, B.L., and T. Gonen. 2016. MicroED opens a new era for biological structure determination. Current Opinions in Structural Biology. 40:128-135

  2. Shi, D., B.L. Nannenga, M.J. de la Cruz, J. Liu, S. Sawtelle, G. Calero, F.E. Reyes, J. Hattne, and T. Gonen. 2016. The collection of MicroED data for macromolecular crystallography. Nature Protocols. 11:895-904


  1. Rodriguez, J.A., M.I. Ivanova, M.R. Sawaya, D. Cascio, F.E. Reyes, D. Shi, S. Sangwan, E.L. Guenther, L.M. Johnson, M. Zheng, L. Jiang, M.A. Arbing, B.L. Nannenga, J. Hattne, J. Whitelegge, A.S. Brewster, M. Messerschmidt, S. Boutet, N.K. Sauter, T. Gonen, and D. Eisenberg. 2015. Structure of the toxic core of α-synuclein from invisible crystals. Nature. 525:486-490

  2. Hattne, J., F.E. Reyes, B.L. Nannenga, D. Shi, J. de la Cruz, A.G.W. Leslie, and T. Gonen. 2015. MicroED data collection and processing. Acta Crystallographica A, Foundation Advances. A71 (Part 4):353-360


  1. Huang, P.S., G. Oberdorfer, C. Xu, X.Y. Pei, B.L. Nannenga, J.M. Rodgers, F. DiMaio, T. Gonen, B. Luisi and D. Baker. 2014. High thermodynamic stability of parametrically designed helical bundles. Science. 346:481-485

  2. Nannenga, B.L., D. Shi, J. Hattne, F.E. Reyes and T. Gonen. 2014. Structure of catalase solved by MicroED. eLife. 3:e03600

  3. Nannenga, B.L.*, D. Shi*, A.G.W. Leslie and T. Gonen. 2014. High-resolution structure determination by continuous-rotation data collection in MicroED. Nature Methods. 11:927-930

  4. Nannenga, B.L. and T. Gonen. 2014. Protein structure determination by MicroED. Current Opinions in Structural Biology. 27:24-31


  1. Shi, D.*, B.L. Nannenga*, M.G. Iadanza* and T. Gonen. 2013. Three-dimensional electron crystallography of protein microcrystals. eLife. 2:e01345

  2. Nannenga, B.L., M.G. Iadanza, B.S. Vollmar and T. Gonen. 2013. Overview of electron crystallography of membrane proteins: Crystallization and screening strategies using negative stain electron microscopy. Current Protocols in Protein Science. 17(15):1-11


Nannenga, B.L. and F. Baneyx. 2012. Folding engineering strategies for efficient membrane protein production in E. coli. Methods in Molecular Biology. 899:187-202


  1. Nannenga, B.L. and F. Baneyx. 2011. Enhanced expression of membrane proteins in E. coli with a PBAD promoter mutant: synergies with chaperone pathway engineering strategies. Microbial Cell Factories. 10:105

  2. Nannenga, B.L. and F. Baneyx. 2011. Reprogramming chaperone pathways to improve membrane protein production in Escherichia coli. Protein Science. 20:1411-1420


  1. Baneyx, F. and B.L. Nannenga. 2010. Chaperones: a story of thrift unfolds. Nature Chemical Biology. 6:880-881

  2. Puertas, J.M.*, B.L. Nannenga*, K.T. Dornfeld, J.M. Betton and F. Baneyx. 2010. Enhancing the secretory yields of leech carboxypeptidase inhibitor in Escherichia coli: influence of trigger factor and signal recognition particle. Protein Expression and Purification. 74:122-128


Kvam, E., B.L. Nannenga, M.S. Wang, Z. Jia, M.R. Sierks and A. Messer. 2009. Conformational targeting of fibrillar polyglutamine proteins in live cells escalates aggregation and cytotoxicity. PLoS ONE. 4:e5727


Nannenga, B.L., A. Zameer and M.R. Sierks. 2008. Anti-oligomeric single chain variable domain antibody differentially affects huntingtin and alpha-synuclien aggregates. FEBS Letters. 582:517-522