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.
Keywords:
Algorithms
,Animals
,Crystallography, X-Ray
,Insect Proteins
,Microscopy, Electron, Scanning
,Silk
,Spiders
,Synchrotrons
,Tensile Strength
,X-Rays