title: X-ray diffraction on spider silk during controlled extrusion under a synchrotron radiation X-ray beam.
abstract: The structure of a single thread of Nephila edulis silk has been studied by in situ X-ray diffraction from a living spider. A systematic increase of orientational order with increasing silking speed up to 40 mm s-1 was observed. Within a few mm from the spinnerets exit, crystalline domains with a beta-poly(L-alanine) structure were observed. The data also suggest an increase in crystalline fraction in the immediate vicinity of the spigot exit.
authors.affiliation: European Synchrotron Radiation Facility, B.P. 220, F-38043 Grenoble, France.
authors.forename: C
authors.initials: C
authors.lastname: Riekel
authors.forename: B
authors.initials: B
authors.lastname: Madsen
authors.forename: D
authors.initials: D
authors.lastname: Knight
authors.forename: F
authors.initials: F
authors.lastname: Vollrath
mesh_terms: D000465:Algorithms; D000818:Animals; D018360:Crystallography, X-Ray; D019476:Insect Proteins / Q000528:radiation effects*; D008855:Microscopy, Electron, Scanning; D047011:Silk; D013112:Spiders / Q000502:physiology*; D017356:Synchrotrons; D013718:Tensile Strength; D014965:X-Rays
chemical_list: D019476:Insect Proteins; D047011:Silk