Fig. 4.

X-ray fibre diffraction provides the characteristic cross-β pattern for amyloid. Top panel shows a schematic showing the features of the cross-β pattern and structure. Lower panels show the cross-β diffraction patterns collected from amyloid fibrils formed by a diverse range of amyloidogenic proteins and peptides. Aβ11–25,^72–74 AAAKKFFEAAAK,⁵² silk,⁷⁵ hIAPP,⁷⁶ NM Sup35,⁷⁷ ccβ,⁷⁸ Met30 TTR,⁷⁹ Tau,⁸⁰ Core PHF,⁸¹ β2M,⁸² Aβ42,^{73, 83} GNNQQNY,⁸⁴ Fibrinogen,⁸⁵ RVFNIM.⁸⁶ Reproduced with permission from ref. 72, copyright 2000 The American Chemical Society.⁷² Reproduced with permission from ref. 73, copyright 2003 Elsevier.⁷³ Reproduced with permission from ref. 74, copyright 2000 Elsevier.⁷⁴ Reproduced with permission from ref. 52, copyright 2005 National Academy of Sciences.⁵² Reproduced with permission from ref. 75, copyright 2007 Wiley-VCH.⁷⁵ Reproduced with permission from ref. 76, copyright 2004 Elsevier.⁷⁶ Reproduced with permission from ref. 77, copyright 2000 American Association for the Advancement of Science.⁷⁷ Reproduced with permission from ref. 78, copyright 2008 Elsevier.⁷⁸ Reproduced with permission from ref. 79, copyright 1996 Ciba Foundation.⁷⁹ Reproduced with permission from ref. 80, copyright 2003 National Academy of Sciences.⁸⁰ Reproduced with permission from ref. 81, copyright 2017 Elsevier.⁸¹ Reproduced with permission from ref. 82, copyright 2008 American Society for Biochemistry and Molecular Biology.⁸² Reproduced with permission from ref. 87, copyright 2012 American Society for Biochemistry and Molecular Biology.⁸⁷ Reproduced with permission from ref. 84, copyright 2010 Elsevier.⁸⁴ Reproduced with permission from ref. 85, copyright 2007 Informa Healthcare.⁸⁵ Reproduced with permission from ref. 86, copyright 2013 Portland Press.⁸⁶