Exploring the amyloid state of proteins by micro

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Micro X-ray Diffractionfor Structural BiologyThe biological problem and ourneed for micro-X-ray diffractionWhat micro-X-ray diffractionhas allowed us to findFuture opportunities for micro-and nano-X-ray diffraction in biology
Amyloid• Unbranched, elongated protein fibrils• Associated with varied diseases (e.g. CJDAlzheimer’s, Dialysis-related amyloidosis)• Cross-β diffraction pattern shows β strandsperpendicular to fiber axis: common spineKishimoto, Namba et al (2004)
Page 1: The Amyloid State of Proteinsand Mi
Page 5 and 6: My Scientific Dilemma in 2001Import
Page 7 and 8: 10-100 mM < 24 hrGNNQQNY microcryst
Page 9 and 10: Packing of GNNQQNY peptides in micr
Page 11 and 12: Microfocus is required to reducebac
Page 13 and 14: GNNQQNY, a dry steric zipperFibers
Page 15 and 16: As of April 2011, ~90 X-raycrystal
Page 17 and 18: D-TLKIVW prevents fibril formation
Page 19 and 20: GGVVIA +JugloneMeytal LandauGGVVIA
Page 21 and 22: Structure of KLVFFA with Orange GKL
Page 23 and 24: Amyloid-like crystalsof KLIMY from
Page 25 and 26: Nano-crystals oflonger (11-residue)
Page 27 and 28: 10 micron Mictigen micromesh in cry
Page 29 and 30: Drosophila crystal cellon 10 µm me
Page 31 and 32: Cell Types Containing Intracellular
Page 33 and 34: The Amyloid State of ProteinsUCLA:

Exploring the amyloid state of proteins by micro

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