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. 2014 Dec 18;9:59. doi: 10.1186/1750-1326-9-59

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© Li et al.; licensee BioMed Central. 2014

This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Bi-lobed models of presenilin 1 complex by electron microscopy. (A) The first bi-lobed structure model of PS1 complex, 14.7 using negative stain EM (EMD-2477). (B) The 4.5 Å model of PS1 complex by cryo-EM (EMD-2677), confirming its bi-lobed shape. (C) 14.7 Å model of PS1 complex bound with its non-transition state inhibitor Compound E (CpdE) (EMD-2478). This model revealed a conformational change induced by the inhibitor.