@article {48265,
	title = {Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED.},
	journal = {Nature Methods},
	volume = {14},
	year = {2017},
	month = {2017 Feb 13},
	pages = {399-402},
	abstract = {<p>Traditionally, crystallographic analysis of macromolecules has depended on large, well-ordered crystals, which often require significant effort to obtain. Even sizable crystals sometimes suffer from pathologies that render them inappropriate for high-resolution structure determination. Here we show that fragmentation of large, imperfect crystals into microcrystals or nanocrystals can provide a simple path for high-resolution structure determination by the cryoEM method MicroED and potentially by serial femtosecond crystallography.</p>
},
	issn = {1548-7105},
	doi = {10.1038/nmeth.4178},
	author = {de la Cruz, M Jason and Hattne, Johan and Shi, Dan and Seidler, Paul and Rodriguez, Jose and Reyes, Francis E and Sawaya, Michael R and Cascio, Duilio and Weiss, Simon C and Kim, Sun Kyung and Hinck, Cynthia S and Hinck, Andrew P and Calero, Guillermo and Eisenberg, David and Gonen, Tamir}
}
@article {48991,
	title = {Common fibrillar spines of amyloid-β and human Islet Amyloid Polypeptide revealed by Micro Electron Diffraction and inhibitors developed using structure-based design.},
	journal = {The Journal of Biological Chemistry},
	volume = {293},
	year = {2017},
	month = {2017 Dec 27},
	pages = {2888-902},
	abstract = {<p>Amyloid-β (Aβ) and human islet amyloid polypeptide (hIAPP) aggregate to form amyloid fibrils that deposit in tissues, and are associated with Alzheimer{\textquoteright}s disease (AD) and Type-II Diabetes (T2D), respectively. Individuals with T2D have an increased risk of developing AD, and conversely, AD patients have an increased risk of developing T2D. Evidence suggests that this link between AD and T2D might originate from a structural similarity between aggregates of Aβ and hIAPP. Using the cryoEM method Micro-Electron Diffraction (MicroED) we determined the atomic structures of 11-residue segments from both Aβ and hIAPP, termed Aβ 24-34 WT and hIAPP 19-29 S20G, with 64\% sequence similarity. We observe a high degree of structural similarity between their backbone atoms (0.96 {\r A} RMSD). Moreover, fibrils of these segments induce amyloid formation through self- and cross-seeding. Furthermore, inhibitors designed for one segment show cross-efficacy for full-length Aβ and hIAPP and reduce cytotoxicity of both proteins, though by apparently blocking different cytotoxic mechanisms. The similarity of the atomic structures of Aβ 24-34 WT and hIAPP 19-29 S20G offers a molecular model for cross-seeding between Aβ and hIAPP.</p>
},
	issn = {1083-351X},
	doi = {10.1074/jbc.M117.806109},
	author = {Krotee, Pascal and Griner, Sarah L and Sawaya, Michael R and Cascio, Duilio and Rodriguez, Jose A and Shi, Dan and Philipp, Stephan and Murray, Kevin and Saelices, Lorena and Lee, Ji and Seidler, Paul and Glabe, Charles G and Jiang, Lin and Gonen, Tamir and Eisenberg, David S}
}
